1cnp: Difference between revisions

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-[[Image:1cnp.gif|left|200px]]<br />
-<applet load="1cnp" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1cnp" />
-'''THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL HOMODIMERIC FOLD FOR S100 CA2+-BINDING PROTEINS, NMR, 22 STRUCTURES'''<br />
-==Overview==
+==THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL HOMODIMERIC FOLD FOR S100 CA2+-BINDING PROTEINS, NMR, 22 STRUCTURES==
-The S100 calcium-binding proteins are implicated as effectors in, calcium-mediated signal transduction pathways. The three-dimensional, structure of the S100 protein calcyclin has been determined in solution in, the apo state by NMR spectroscopy and a computational strategy that, incorporates a systematic docking protocol. This structure reveals a, symmetric homodimeric fold that is unique among calcium-binding proteins., Dimerization is mediated by hydrophobic contacts from several highly, conserved residues, which suggests that the dimer fold identified for, calcyclin will serve as a structural paradigm for the S100 subfamily of, calcium-binding proteins.
+<StructureSection load='1cnp' size='340' side='right'caption='[[1cnp]]' scene=''>
+== Structural highlights ==
+<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>
+</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=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>
+== 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/cn/1cnp_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=1cnp ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The S100 calcium-binding proteins are implicated as effectors in calcium-mediated signal transduction pathways. The three-dimensional structure of the S100 protein calcyclin has been determined in solution in the apo state by NMR spectroscopy and a computational strategy that incorporates a systematic docking protocol. This structure reveals a symmetric homodimeric fold that is unique among calcium-binding proteins. Dimerization is mediated by hydrophobic contacts from several highly conserved residues, which suggests that the dimer fold identified for calcyclin will serve as a structural paradigm for the S100 subfamily of calcium-binding proteins.
-==About this Structure==
+The structure of calcyclin reveals a novel homodimeric fold for S100 Ca(2+)-binding proteins.,Potts BC, Smith J, Akke M, Macke TJ, Okazaki K, Hidaka H, Case DA, Chazin WJ Nat Struct Biol. 1995 Sep;2(9):790-6. PMID:7552751<ref>PMID:7552751</ref>
-CNP is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]]. Structure known Active Sites: LO1, LO2, LO3 and LO4. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CNP OCA]].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-The structure of calcyclin reveals a novel homodimeric fold for S100 Ca(2+)-binding proteins., Potts BC, Smith J, Akke M, Macke TJ, Okazaki K, Hidaka H, Case DA, Chazin WJ, Nat Struct Biol. 1995 Sep;2(9):790-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7552751 7552751]
+</div>
+<div class="pdbe-citations 1cnp" 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: Akke M]]
-[[Category: Akke, M.]]
+[[Category: Case DA]]
-[[Category: Case, D.A.]]
+[[Category: Chazin WJ]]
-[[Category: Chazin, W.J.]]
+[[Category: Hidaka H]]
-[[Category: Hidaka, H.]]
+[[Category: Macke TJ]]
-[[Category: Macke, T.J.]]
+[[Category: Okazaki K]]
-[[Category: Okazaki, K.]]
+[[Category: Potts BCM]]
-[[Category: Potts, B.C.M.]]
+[[Category: Smith J]]
-[[Category: Smith, J.]]
-[[Category: calcium-binding protein]]
-[[Category: ef-hand]]
-[[Category: s-100 protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:08:27 2007''