3mce: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
 ==Crystal structure of the NAC domain of alpha subunit of nascent polypeptide-associated complex(NAC)==
-<StructureSection load='3mce' size='340' side='right' caption='[[3mce]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+<StructureSection load='3mce' size='340' side='right'caption='[[3mce]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3mce]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MCE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MCE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3mce]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MCE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MCE FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.396&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mcb|3mcb]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Alpha NAC, HSD48, NACA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3mce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mce OCA], [https://pdbe.org/3mce PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mce RCSB], [https://www.ebi.ac.uk/pdbsum/3mce PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mce ProSAT]</span></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=3mce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mce OCA], [http://pdbe.org/3mce PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mce RCSB], [http://www.ebi.ac.uk/pdbsum/3mce PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mce ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/NACA_HUMAN NACA_HUMAN]] Prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. Also reduces the inherent affinity of ribosomes for protein translocation sites in the ER membrane (M sites). May act as a specific coactivator for JUN, binding to DNA and stabilizing the interaction of JUN homodimers with target gene promoters.<ref>PMID:9877153</ref> <ref>PMID:10982809</ref> <ref>PMID:15784678</ref>
+[https://www.uniprot.org/uniprot/NACA_HUMAN NACA_HUMAN] Prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. Also reduces the inherent affinity of ribosomes for protein translocation sites in the ER membrane (M sites). May act as a specific coactivator for JUN, binding to DNA and stabilizing the interaction of JUN homodimers with target gene promoters.<ref>PMID:9877153</ref> <ref>PMID:10982809</ref> <ref>PMID:15784678</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mc/3mce_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mc/3mce_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 21: / Line 20: @@
 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3mce ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Nascent polypeptide associated complex (NAC) and its two isolated subunits, alphaNAC and betaNAC, play important roles in nascent peptide targeting. We determined a 1.9 A resolution crystal structure of the interaction core of NAC heterodimer and a 2.4 A resolution crystal structure of alphaNAC NAC domain homodimer. These structures provide detailed information of NAC heterodimerization and alphaNAC homodimerization. We found that the NAC domains of alphaNAC and betaNAC share very similar folding despite of their relative low identity of amino acid sequences. Furthermore, different electric charge distributions of the two subunits at the NAC interface provide an explanation to the observation that the heterodimer of NAC complex is more stable than the single subunit homodimer. In addition, we successfully built a betaNAC NAC domain homodimer model based on homologous modeling, suggesting that NAC domain dimerization is a general property of the NAC family. These 3D structures allow further studies on structure-function relationship of NAC.
-Crystal structures of NAC domains of human nascent polypeptide-associated complex (NAC) and its alphaNAC subunit.,Wang L, Zhang W, Wang L, Zhang XC, Li X, Rao Z Protein Cell. 2010 Apr;1(4):406-16. Epub 2010 May 8. PMID:21203952<ref>PMID:21203952</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3mce" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Li, X M]]
+[[Category: Large Structures]]
-[[Category: Rao, Z]]
+[[Category: Li XM]]
-[[Category: Wang, L]]
+[[Category: Rao Z]]
-[[Category: Wang, L F]]
+[[Category: Wang L]]
-[[Category: Zhang, W C]]
+[[Category: Wang LF]]
-[[Category: Zhang, X J.C]]
+[[Category: Zhang WC]]
-[[Category: Beta-barrel like structure]]
+[[Category: Zhang XJC]]
-[[Category: Chaperone]]
-[[Category: Homodimer]]
-[[Category: Nac]]