1cnp

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==THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL HOMODIMERIC FOLD FOR S100 CA2+-BINDING PROTEINS, NMR, 22 STRUCTURES==
==THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL HOMODIMERIC FOLD FOR S100 CA2+-BINDING PROTEINS, NMR, 22 STRUCTURES==
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<StructureSection load='1cnp' size='340' side='right' caption='[[1cnp]], [[NMR_Ensembles_of_Models | 22 NMR models]]' scene=''>
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<StructureSection load='1cnp' size='340' side='right'caption='[[1cnp]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1cnp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CNP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CNP FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1cnp]] 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=1CNP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CNP FirstGlance]. <br>
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</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=1cnp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cnp OCA], [http://pdbe.org/1cnp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cnp RCSB], [http://www.ebi.ac.uk/pdbsum/1cnp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cnp ProSAT]</span></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">Solution NMR</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=1cnp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cnp OCA], [https://pdbe.org/1cnp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cnp RCSB], [https://www.ebi.ac.uk/pdbsum/1cnp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cnp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/S10A6_RABIT S10A6_RABIT]] May function as calcium sensor and contribute to cellular calcium signaling (Potential). May function by interacting with other proteins and indirectly play a role in the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative (By similarity). Interacts with FKBP4 (By similarity).
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[https://www.uniprot.org/uniprot/S10A6_RABIT S10A6_RABIT] May function as calcium sensor and contribute to cellular calcium signaling (Potential). May function by interacting with other proteins and indirectly play a role in the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative (By similarity). Interacts with FKBP4 (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cn/1cnp_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cn/1cnp_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
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</div>
</div>
<div class="pdbe-citations 1cnp" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 1cnp" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[S100 proteins 3D structures|S100 proteins 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Akke, M]]
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[[Category: Akke M]]
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[[Category: Case, D A]]
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[[Category: Case DA]]
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[[Category: Chazin, W J]]
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[[Category: Chazin WJ]]
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[[Category: Hidaka, H]]
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[[Category: Hidaka H]]
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[[Category: Macke, T J]]
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[[Category: Macke TJ]]
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[[Category: Okazaki, K]]
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[[Category: Okazaki K]]
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[[Category: Potts, B C.M]]
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[[Category: Potts BCM]]
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[[Category: Smith, J]]
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[[Category: Smith J]]
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[[Category: Calcium-binding protein]]
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[[Category: Ef-hand]]
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[[Category: S-100 protein]]
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Current revision

THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL HOMODIMERIC FOLD FOR S100 CA2+-BINDING PROTEINS, NMR, 22 STRUCTURES

PDB ID 1cnp

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