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1nsh

From Proteopedia

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[[Image:1nsh.gif|left|200px]]
 
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{{Structure
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==Solution Structure of Rabbit apo-S100A11 (19 models)==
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|PDB= 1nsh |SIZE=350|CAPTION= <scene name='initialview01'>1nsh</scene>
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<StructureSection load='1nsh' size='340' side='right'caption='[[1nsh]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE= S100A11 OR S100C OR PCALG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 Oryctolagus cuniculus])
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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=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>
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}}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/S10AB_RABIT S10AB_RABIT] Facilitates the differentiation and the cornification of keratinocytes (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ns/1nsh_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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'''Solution Structure of Rabbit apo-S100A11 (19 models)'''
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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&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 1nsh" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[S100 proteins 3D structures|S100 proteins 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1NSH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NSH OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12842051 12842051]
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[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Single protein]]
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[[Category: Dempsey AC]]
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[[Category: Dempsey, A C.]]
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[[Category: Shaw GS]]
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[[Category: Shaw, G S.]]
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[[Category: Walsh MP]]
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[[Category: Walsh, M P.]]
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[[Category: calcium-binding protein]]
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[[Category: ef hand]]
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[[Category: helix-loop-helix]]
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[[Category: s100a11]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:01:05 2008''
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Current revision

Solution Structure of Rabbit apo-S100A11 (19 models)

PDB ID 1nsh

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