|
|
| (3 intermediate revisions by the same user not shown) |
| Line 1: |
Line 1: |
| | |
| ==Mammalian 40S HCV-IRES complex== | | ==Mammalian 40S HCV-IRES complex== |
| <StructureSection load='5flx' size='340' side='right' caption='[[5flx]], [[Resolution|resolution]] 3.90Å' scene=''> | | <SX load='5flx' size='340' side='right' viewer='molstar' caption='[[5flx]], [[Resolution|resolution]] 3.90Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[5flx]] is a 35 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FLX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FLX FirstGlance]. <br> | | <table><tr><td colspan='2'>[[5flx]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FLX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FLX FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.9Å</td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-(apurinic_or_apyrimidinic_site)_lyase DNA-(apurinic or apyrimidinic site) lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.99.18 4.2.99.18] </span></td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5flx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5flx OCA], [http://pdbe.org/5flx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5flx RCSB], [http://www.ebi.ac.uk/pdbsum/5flx PDBsum]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5flx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5flx OCA], [https://pdbe.org/5flx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5flx RCSB], [https://www.ebi.ac.uk/pdbsum/5flx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5flx ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Disease ==
| |
| [[http://www.uniprot.org/uniprot/RS19_HUMAN RS19_HUMAN]] Blackfan-Diamond disease. Diamond-Blackfan anemia 1 (DBA1) [MIM:[http://omim.org/entry/105650 105650]]: A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of developing leukemia. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:17517689</ref> <ref>PMID:12586610</ref> <ref>PMID:9988267</ref> <ref>PMID:10590074</ref> <ref>PMID:11112378</ref> <ref>PMID:12750732</ref> <ref>PMID:15384984</ref> [REFERENCE:18] [[http://www.uniprot.org/uniprot/RS24_HUMAN RS24_HUMAN]] Blackfan-Diamond disease. Diamond-Blackfan anemia 3 (DBA3) [MIM:[http://omim.org/entry/610629 610629]]: A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of developing leukemia. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:17186470</ref> [[http://www.uniprot.org/uniprot/RS14_HUMAN RS14_HUMAN]] Myelodysplastic syndrome associated with isolated del(5q) chromosome abnormality. [[http://www.uniprot.org/uniprot/RS26_HUMAN RS26_HUMAN]] Blackfan-Diamond disease. Diamond-Blackfan anemia 10 (DBA10) [MIM:[http://omim.org/entry/613309 613309]]: A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:20116044</ref> [[http://www.uniprot.org/uniprot/RS7_HUMAN RS7_HUMAN]] Blackfan-Diamond disease. Diamond-Blackfan anemia 8 (DBA8) [MIM:[http://omim.org/entry/612563 612563]]: A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:19061985</ref> [[http://www.uniprot.org/uniprot/RS10_HUMAN RS10_HUMAN]] Blackfan-Diamond disease. Diamond-Blackfan anemia 9 (DBA9) [MIM:[http://omim.org/entry/613308 613308]]: A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:20116044</ref> [[http://www.uniprot.org/uniprot/RS17_HUMAN RS17_HUMAN]] Blackfan-Diamond disease. Diamond-Blackfan anemia 4 (DBA4) [MIM:[http://omim.org/entry/612527 612527]]: A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of developing leukemia. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:17647292</ref> <ref>PMID:19061985</ref>
| |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/RS27A_HUMAN RS27A_HUMAN]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref> Ribosomal protein S27a is a component of the 40S subunit of the ribosome.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref> [[http://www.uniprot.org/uniprot/RS19_HUMAN RS19_HUMAN]] Required for pre-rRNA processing and maturation of 40S ribosomal subunits.<ref>PMID:16990592</ref> [[http://www.uniprot.org/uniprot/RS24_HUMAN RS24_HUMAN]] Required for processing of pre-rRNA and maturation of 40S ribosomal subunits.<ref>PMID:18230666</ref> [[http://www.uniprot.org/uniprot/RSSA_HUMAN RSSA_HUMAN]] Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis. Acts as a PPP1R16B-dependent substrate of PPP1CA. Also acts as a receptor for several other ligands, including the pathogenic prion protein, viruses, and bacteria.<ref>PMID:6300843</ref> <ref>PMID:16263087</ref> <ref>PMID:15516338</ref> [[http://www.uniprot.org/uniprot/RS18_HUMAN RS18_HUMAN]] Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA (By similarity).[HAMAP-Rule:MF_01315] [[http://www.uniprot.org/uniprot/RS3A_HUMAN RS3A_HUMAN]] May play a role during erythropoiesis through regulation of transcription factor DDIT3 (By similarity).[HAMAP-Rule:MF_03122] [[http://www.uniprot.org/uniprot/RS7_HUMAN RS7_HUMAN]] Required for rRNA maturation.<ref>PMID:19061985</ref> [[http://www.uniprot.org/uniprot/RS10_HUMAN RS10_HUMAN]] Component of the 40S ribosomal subunit. [[http://www.uniprot.org/uniprot/RS6_HUMAN RS6_HUMAN]] May play an important role in controlling cell growth and proliferation through the selective translation of particular classes of mRNA. [[http://www.uniprot.org/uniprot/GBLP_HUMAN GBLP_HUMAN]] Involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression. Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation. May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6. Inhibits the activity of SRC kinases including SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer. Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix. Involved in PKC-dependent translocation of ADAM12 to the cell membrane. Promotes the ubiquitination and proteasome-mediated degradation of proteins such as CLEC1B and HIF1A. Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation. Required for PTK2/FAK1 phosphorylation and dephosphorylation. Regulates internalization of the muscarinic receptor CHRM2. Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity. Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a role in regulation of FLT1-mediated cell migration. Binds to Y.pseudotuberculosis yopK which leads to inhibition of phagocytosis and survival of bacteria following infection of host cells. Enhances phosphorylation of HIV-1 Nef by PKCs. Promotes migration of breast carcinoma cells by binding to and activating RHOA.<ref>PMID:9584165</ref> <ref>PMID:11312657</ref> <ref>PMID:11884618</ref> <ref>PMID:12958311</ref> <ref>PMID:12589061</ref> <ref>PMID:17108144</ref> <ref>PMID:17956333</ref> <ref>PMID:17244529</ref> <ref>PMID:18258429</ref> <ref>PMID:18621736</ref> <ref>PMID:18088317</ref> <ref>PMID:19785988</ref> <ref>PMID:19423701</ref> <ref>PMID:20541605</ref> <ref>PMID:20976005</ref> <ref>PMID:20573744</ref> <ref>PMID:20499158</ref> <ref>PMID:21212275</ref> <ref>PMID:21347310</ref> | | [https://www.uniprot.org/uniprot/RS3_HUMAN RS3_HUMAN] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 20: |
Line 19: |
| </div> | | </div> |
| <div class="pdbe-citations 5flx" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5flx" style="background-color:#fffaf0;"></div> |
| | |
| | ==See Also== |
| | *[[3D sructureseceptor for activated protein kinase C 1|3D sructureseceptor for activated protein kinase C 1]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </SX> |
| | [[Category: Large Structures]] |
| [[Category: Oryctolagus cuniculus]] | | [[Category: Oryctolagus cuniculus]] |
| [[Category: Burger, J]] | | [[Category: Burger J]] |
| [[Category: Collier, M]] | | [[Category: Collier M]] |
| [[Category: Dabrowski, M]] | | [[Category: Dabrowski M]] |
| [[Category: Hilal, T]] | | [[Category: Hilal T]] |
| [[Category: Hildebrand, P W]] | | [[Category: Hildebrand PW]] |
| [[Category: Ismer, J]] | | [[Category: Ismer J]] |
| [[Category: Loerke, J]] | | [[Category: Loerke J]] |
| [[Category: Mielke, T]] | | [[Category: Mielke T]] |
| [[Category: Scheerer, P]] | | [[Category: Scheerer P]] |
| [[Category: Schmidt, A]] | | [[Category: Schmidt A]] |
| [[Category: Shaikh, T R]] | | [[Category: Shaikh TR]] |
| [[Category: Spahn, C M.T]] | | [[Category: Spahn CMT]] |
| [[Category: Sprink, T]] | | [[Category: Sprink T]] |
| [[Category: Yamamoto, H]] | | [[Category: Yamamoto H]] |
| [[Category: Yamamoto, K]] | | [[Category: Yamamoto K]] |
| [[Category: Hepatitis c virus internal ribosome entry site]]
| |
| [[Category: Ribosome]]
| |
| [[Category: Translation initiation]]
| |