1nsh
From Proteopedia
(Difference between revisions)
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==Solution Structure of Rabbit apo-S100A11 (19 models)== | ==Solution Structure of Rabbit apo-S100A11 (19 models)== | ||
| - | <StructureSection load='1nsh' size='340' side='right'caption='[[1nsh | + | <StructureSection load='1nsh' size='340' side='right'caption='[[1nsh]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1nsh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1nsh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NSH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NSH FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1nsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nsh OCA], [https://pdbe.org/1nsh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nsh RCSB], [https://www.ebi.ac.uk/pdbsum/1nsh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nsh 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=1nsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nsh OCA], [https://pdbe.org/1nsh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nsh RCSB], [https://www.ebi.ac.uk/pdbsum/1nsh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nsh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/S10AB_RABIT S10AB_RABIT] Facilitates the differentiation and the cornification of keratinocytes (By similarity). | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=1nsh ConSurf]. | </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=1nsh ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | S100A11 is a homodimeric EF-hand calcium binding protein that undergoes a calcium-induced conformational change and interacts with the phospholipid binding protein annexin I to coordinate membrane association. In this work, the solution structure of apo-S100A11 has been determined by NMR spectroscopy to uncover the details of its calcium-induced structural change. Apo-S100A11 forms a tight globular structure having a near antiparallel orientation of helices III and IV in calcium binding site II. Further, helices I and IV, and I and I', form a more closed arrangement than observed in other apo-S100 proteins. This helix arrangement in apo-S100A11 partially buries residues in helices I (P3, E11, A15), III (V55, R58, M59), and IV (A86, C87, S90) and the linker (A45, F46), which are required for interaction with annexin I in the calcium-bound state. In apo-S100A11, this results in a "masked" binding surface that prevents annexin I binding but is uncovered upon calcium binding. | ||
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| - | Unmasking the annexin I interaction from the structure of Apo-S100A11.,Dempsey AC, Walsh MP, Shaw GS Structure. 2003 Jul;11(7):887-97. PMID:12842051<ref>PMID:12842051</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1nsh" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[S100 proteins 3D structures|S100 proteins 3D structures]] | *[[S100 proteins 3D structures|S100 proteins 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: European rabbit]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Oryctolagus cuniculus]] |
| - | [[Category: | + | [[Category: Dempsey AC]] |
| - | [[Category: | + | [[Category: Shaw GS]] |
| - | [[Category: | + | [[Category: Walsh MP]] |
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Revision as of 08:52, 10 April 2024
Solution Structure of Rabbit apo-S100A11 (19 models)
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