1jwd: Difference between revisions

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-[[Image:1jwd.gif|left|200px]]<br /><applet load="1jwd" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1jwd" />
-'''Ca2+-induced Structural Changes in Calcyclin: High-resolution Solution Structure of Ca2+-bound Calcyclin.'''<br />
-==Overview==
+==Ca2+-induced Structural Changes in Calcyclin: High-resolution Solution Structure of Ca2+-bound Calcyclin.==
-Calcyclin is a homodimeric protein belonging to the S100 subfamily of, EF-hand Ca(2+)-binding proteins, which function in Ca(2+) signal, transduction processes. A refined high-resolution solution structure of, Ca(2+)-bound rabbit calcyclin has been determined by heteronuclear, solution NMR. In order to understand the Ca(2+)-induced structural changes, in S100 proteins, in-depth comparative structural analyses were used to, compare the apo and Ca(2+)-bound states of calcyclin, the closely related, S100B, and the prototypical Ca(2+)-sensor protein calmodulin. Upon Ca(2+), binding, the position and orientation of helix III in the second EF-hand, is altered, whereas the rest of the protein, including the dimer, interface, remains virtually unchanged. This Ca(2+)-induced structural, change is much less drastic than the "opening" of the globular EF-hand, domains that occurs in classical Ca(2+) sensors, such as calmodulin. Using, homology models of calcyclin based on S100B, a binding site in calcyclin, has been proposed for the N-terminal domain of annexin XI and the, C-terminal domain of the neuronal calcyclin-binding protein. The, structural basis for the specificity of S100 proteins is discussed in, terms of the variation in sequence of critical contact residues in the, common S100 target-binding site.
+<StructureSection load='1jwd' size='340' side='right'caption='[[1jwd]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1jwd]] 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=1JWD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JWD FirstGlance]. <br>
+</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=1jwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jwd OCA], [https://pdbe.org/1jwd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jwd RCSB], [https://www.ebi.ac.uk/pdbsum/1jwd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jwd ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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 ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jw/1jwd_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1jwd ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Calcyclin is a homodimeric protein belonging to the S100 subfamily of EF-hand Ca(2+)-binding proteins, which function in Ca(2+) signal transduction processes. A refined high-resolution solution structure of Ca(2+)-bound rabbit calcyclin has been determined by heteronuclear solution NMR. In order to understand the Ca(2+)-induced structural changes in S100 proteins, in-depth comparative structural analyses were used to compare the apo and Ca(2+)-bound states of calcyclin, the closely related S100B, and the prototypical Ca(2+)-sensor protein calmodulin. Upon Ca(2+) binding, the position and orientation of helix III in the second EF-hand is altered, whereas the rest of the protein, including the dimer interface, remains virtually unchanged. This Ca(2+)-induced structural change is much less drastic than the "opening" of the globular EF-hand domains that occurs in classical Ca(2+) sensors, such as calmodulin. Using homology models of calcyclin based on S100B, a binding site in calcyclin has been proposed for the N-terminal domain of annexin XI and the C-terminal domain of the neuronal calcyclin-binding protein. The structural basis for the specificity of S100 proteins is discussed in terms of the variation in sequence of critical contact residues in the common S100 target-binding site.
-==About this Structure==
+A structural basis for S100 protein specificity derived from comparative analysis of apo and Ca(2+)-calcyclin.,Maler L, Sastry M, Chazin WJ J Mol Biol. 2002 Mar 22;317(2):279-90. PMID:11902843<ref>PMID:11902843</ref>
-JWD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JWD OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-A structural basis for S100 protein specificity derived from comparative analysis of apo and Ca(2+)-calcyclin., Maler L, Sastry M, Chazin WJ, J Mol Biol. 2002 Mar 22;317(2):279-90. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11902843 11902843]
+</div>
+<div class="pdbe-citations 1jwd" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[S100 proteins 3D structures|S100 proteins 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Oryctolagus cuniculus]]
-[[Category: Single protein]]
+[[Category: Chazin WJ]]
-[[Category: Chazin, W.J.]]
+[[Category: Maler L]]
-[[Category: Maler, L.]]
+[[Category: Sastry M]]
-[[Category: Sastry, M.]]
-[[Category: ca(2+)-binding protein]]
-[[Category: ef-hand]]
-[[Category: s100 protein]]
-[[Category: s100a6]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:38:12 2007''