3qca

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Current revision (08:34, 20 March 2024) (edit) (undo)
 
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<StructureSection load='3qca' size='340' side='right'caption='[[3qca]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='3qca' size='340' side='right'caption='[[3qca]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qca]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QCA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QCA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qca]] 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=3QCA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QCA FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3qc8|3qc8]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FAF1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qca OCA], [https://pdbe.org/3qca PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qca RCSB], [https://www.ebi.ac.uk/pdbsum/3qca PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qca ProSAT]</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=3qca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qca OCA], [https://pdbe.org/3qca PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qca RCSB], [https://www.ebi.ac.uk/pdbsum/3qca PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qca ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/FAF1_HUMAN FAF1_HUMAN]] Potentiates but cannot initiate FAS-induced apoptosis.
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[https://www.uniprot.org/uniprot/FAF1_HUMAN FAF1_HUMAN] Potentiates but cannot initiate FAS-induced apoptosis.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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UBX domain is a general p97/VCP-binding module found in an increasing number of proteins including FAF1, p47, SAKS1 and UBXD7. FAF1, a multi-functional tumor suppressor protein, binds to the N domain of p97/VCP through its C-terminal UBX domain and thereby inhibits the proteasomal protein degradation in which p97/VCP acts as a co-chaperone. Here we report the crystal structure of human FAF1 UBX domain at 2.9A resolution. It reveals that the conserved FP sequence in the p97/VCP-binding region adopts a rarely observed cis-Pro touch-turn structure. We call it an FcisP touch-turn motif and suggest that it is the conserved structural element of the UBX domain. Four FAF1 UBX molecules in an asymmetric unit of the crystal show two different conformations of the FcisP touch-turn motif. The phenyl ring of F(619) in the motif stacks partly over cis-Pro(620) in one conformation, whereas it is swung out from cis-P(620), in the other conformation, and forms hydrophobic contacts with the residues of the neighboring molecule. In addition, the entire FcisP touch-turn motif is pulled out in the second conformation by about 2A in comparison to the first conformation. Those conformational differences observed in the p97/VCP-binding motif caused by the interaction with neighboring molecules presumably represent the conformational change of the UBX domain on its binding to the N domain of p97/VCP.
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Crystal structure of human FAF1 UBX domain reveals a novel FcisP touch-turn motif in p97/VCP-binding region.,Kang W, Yang JK Biochem Biophys Res Commun. 2011 Apr 15;407(3):531-4. Epub 2011 Mar 23. PMID:21414298<ref>PMID:21414298</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3qca" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Kang, W]]
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[[Category: Kang W]]
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[[Category: Kim, K H]]
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[[Category: Kim KH]]
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[[Category: Suh, S W]]
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[[Category: Suh SW]]
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[[Category: Yang, J K]]
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[[Category: Yang JK]]
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[[Category: Faf1]]
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[[Category: Protein binding]]
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[[Category: Ubx]]
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Current revision

Crystal Structure of FAF1 UBX Domain In Complex with p97/VCP N Domain Reveals The Conserved FcisP Touch-Turn Motif of UBX Domain Suffering Conformational Change

PDB ID 3qca

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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