1d1o: Difference between revisions

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-[[Image:1d1o.jpg|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1d1o", creates the "Structure Box" on the page.
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-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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-{{STRUCTURE_1d1o|  PDB=1d1o  |  SCENE=  }}
-'''COOPERATIVITY IN EF-HAND CA2+-BINDING PROTEINS: EVIDENCE OF SITE-SITE COMMUNICATION FROM BINDING-INDUCED CHANGES IN STRUCTURE AND DYNAMICS OF N56A CALBINDIN D9K'''
+==COOPERATIVITY IN EF-HAND CA2+-BINDING PROTEINS: EVIDENCE OF SITE-SITE COMMUNICATION FROM BINDING-INDUCED CHANGES IN STRUCTURE AND DYNAMICS OF N56A CALBINDIN D9K==
+<StructureSection load='1d1o' size='340' side='right'caption='[[1d1o]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1d1o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D1O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D1O 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=1d1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d1o OCA], [https://pdbe.org/1d1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d1o RCSB], [https://www.ebi.ac.uk/pdbsum/1d1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d1o ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/S100G_BOVIN S100G_BOVIN]
+== 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/d1/1d1o_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=1d1o ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The cooperative binding of Ca2+ ions is an essential functional property of the EF-hand family of Ca2+-binding proteins. To understand how these proteins function, it is essential to characterize intermediate binding states in addition to the apo- and holo-proteins. The three-dimensional solution structure and fast time scale internal motional dynamics of the backbone have been determined for the half-saturated state of the N56A mutant of calbindin D9k with Ca2+ bound only in the N-terminal site. The extent of conformational reorganization and a loss of flexibility in the C-terminal EF-hand upon binding of an ion in the N-terminal EF-hand provide clear evidence of the importance of site-site interactions in this family of proteins, and demonstrates the strength of long-range effects in the cooperative EF-hand Ca2+-binding domain.
-==Overview==
+Site-site communication in the EF-hand Ca2+-binding protein calbindin D9k.,Maler L, Blankenship J, Rance M, Chazin WJ Nat Struct Biol. 2000 Mar;7(3):245-50. PMID:10700285<ref>PMID:10700285</ref>
-The cooperative binding of Ca2+ ions is an essential functional property of the EF-hand family of Ca2+-binding proteins. To understand how these proteins function, it is essential to characterize intermediate binding states in addition to the apo- and holo-proteins. The three-dimensional solution structure and fast time scale internal motional dynamics of the backbone have been determined for the half-saturated state of the N56A mutant of calbindin D9k with Ca2+ bound only in the N-terminal site. The extent of conformational reorganization and a loss of flexibility in the C-terminal EF-hand upon binding of an ion in the N-terminal EF-hand provide clear evidence of the importance of site-site interactions in this family of proteins, and demonstrates the strength of long-range effects in the cooperative EF-hand Ca2+-binding domain.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-D1O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D1O OCA].
+</div>
+<div class="pdbe-citations 1d1o" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Site-site communication in the EF-hand Ca2+-binding protein calbindin D9k., Maler L, Blankenship J, Rance M, Chazin WJ, Nat Struct Biol. 2000 Mar;7(3):245-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10700285 10700285]
+*[[S100 proteins 3D structures|S100 proteins 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Bos taurus]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Blankenship, J.]]
+[[Category: Blankenship J]]
-[[Category: Chazin, W J.]]
+[[Category: Chazin WJ]]
-[[Category: Maler, L.]]
+[[Category: Maler L]]
-[[Category: Rance, M.]]
+[[Category: Rance M]]
-[[Category: Calcium-binding protein]]
-[[Category: Ef-hand]]
-[[Category: Nmr]]
-[[Category: Signal transduction]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:20:55 2008''