|
|
(One intermediate revision by the same user not shown) |
Line 1: |
Line 1: |
|
| |
|
| ==Crystal structure of the His Domain Protein Tyrosine Phosphatase (HD-PTP/PTPN23) Bro1 domain (CHMP4B peptide complex structure)== | | ==Crystal structure of the His Domain Protein Tyrosine Phosphatase (HD-PTP/PTPN23) Bro1 domain (CHMP4B peptide complex structure)== |
| <StructureSection load='5mk2' size='340' side='right' caption='[[5mk2]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='5mk2' size='340' side='right'caption='[[5mk2]], [[Resolution|resolution]] 1.70Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[5mk2]] is a 3 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=5MK2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MK2 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[5mk2]] is a 3 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=5MK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MK2 FirstGlance]. <br> |
| </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTPN23, KIAA1471 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]] 1.7Å</td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </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=5mk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mk2 OCA], [https://pdbe.org/5mk2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mk2 RCSB], [https://www.ebi.ac.uk/pdbsum/5mk2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mk2 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=5mk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mk2 OCA], [http://pdbe.org/5mk2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mk2 RCSB], [http://www.ebi.ac.uk/pdbsum/5mk2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mk2 ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Disease ==
| |
| [[http://www.uniprot.org/uniprot/CHM4B_HUMAN CHM4B_HUMAN]] Defects in CHMP4B are the cause of cataract posterior polar type 3 (CTPP3) [MIM:[http://omim.org/entry/605387 605387]]. A subcapsular opacity, usually disk-shaped, located at the back of the lens. It can have a marked effect on visual acuity.<ref>PMID:17701905</ref>
| |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/PTN23_HUMAN PTN23_HUMAN]] Plays a role in sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs) via its interaction with the ESCRT-I complex (endosomal sorting complex required for transport I), and possibly also other ESCRT complexes. May act as a negative regulator of Ras-mediated mitogenic activity. Plays a role in ciliogenesis.<ref>PMID:18434552</ref> <ref>PMID:20393563</ref> <ref>PMID:21757351</ref> [[http://www.uniprot.org/uniprot/CHM4B_HUMAN CHM4B_HUMAN]] Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. When overexpressed, membrane-assembled circular arrays of CHMP4B filaments can promote or stabilize negative curvature and outward budding. Via its interaction with PDCD6IP involved in HIV-1 p6- and p9-dependent virus release.<ref>PMID:12860994</ref> <ref>PMID:14505569</ref> <ref>PMID:14505570</ref> <ref>PMID:14519844</ref> <ref>PMID:18209100</ref> | | [https://www.uniprot.org/uniprot/PTN23_HUMAN PTN23_HUMAN] Plays a role in sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs) via its interaction with the ESCRT-I complex (endosomal sorting complex required for transport I), and possibly also other ESCRT complexes. May act as a negative regulator of Ras-mediated mitogenic activity. Plays a role in ciliogenesis.<ref>PMID:18434552</ref> <ref>PMID:20393563</ref> <ref>PMID:21757351</ref> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
Line 21: |
Line 18: |
| </div> | | </div> |
| <div class="pdbe-citations 5mk2" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5mk2" style="background-color:#fffaf0;"></div> |
| | |
| | ==See Also== |
| | *[[Charged multivesicular body protein 3D structures|Charged multivesicular body protein 3D structures]] |
| | *[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Human]] | | [[Category: Homo sapiens]] |
| [[Category: Protein-tyrosine-phosphatase]] | | [[Category: Large Structures]] |
| [[Category: Gahloth, D]] | | [[Category: Gahloth D]] |
| [[Category: Levy, C]] | | [[Category: Levy C]] |
| [[Category: Escrt-iii chmp4b]]
| |
| [[Category: Hydrolase]]
| |