1b8c: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1b8c.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1b8c", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
--->
-{{STRUCTURE_1b8c|  PDB=1b8c  |  SCENE=  }}
-'''PARVALBUMIN'''
+==PARVALBUMIN==
+<StructureSection load='1b8c' size='340' side='right'caption='[[1b8c]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1b8c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cyprinus_carpio Cyprinus carpio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B8C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B8C FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=1b8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b8c OCA], [https://pdbe.org/1b8c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b8c RCSB], [https://www.ebi.ac.uk/pdbsum/1b8c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b8c ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PRVB_CYPCA PRVB_CYPCA] In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions.
+== 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/b8/1b8c_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=1b8c ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+BACKGROUND: The EF-hand family is a large set of Ca(2+)-binding proteins that contain characteristic helix-loop-helix binding motifs that are highly conserved in sequence. Members of this family include parvalbumin and many prominent regulatory proteins such as calmodulin and troponin C. EF-hand proteins are involved in a variety of physiological processes including cell-cycle regulation, second messenger production, muscle contraction, microtubule organization and vision. RESULTS: We have determined the structures of parvalbumin mutants designed to explore the role of the last coordinating residue of the Ca(2+)-binding loop. An E101D substitution has been made in the parvalbumin EF site. The substitution decreases the Ca(2+)-binding affinity 100-fold and increases the Mg(2+)-binding affinity 10-fold. Both the Ca(2+)- and Mg(2+)-bound structures have been determined, and a structural basis has been proposed for the metal-ion-binding properties. CONCLUSIONS: The E101D mutation does not affect the Mg(2+) coordination geometry of the binding loop, but it does pull the F helix 1.1 A towards the loop. The E101D-Ca(2+) structure reveals that this mutant cannot obtain the sevenfold coordination preferred by Ca(2+), presumably because of strain limits imposed by tertiary structure. Analysis of these results relative to previously reported structural information supports a model wherein the characteristics of the last coordinating residue and the plasticity of the Ca(2+)-binding loop delimit the allowable geometries for the coordinating sphere.
-==Overview==
+Metal-ion affinity and specificity in EF-hand proteins: coordination geometry and domain plasticity in parvalbumin.,Cates MS, Berry MB, Ho EL, Li Q, Potter JD, Phillips GN Jr Structure. 1999 Oct 15;7(10):1269-78. PMID:10545326<ref>PMID:10545326</ref>
-BACKGROUND: The EF-hand family is a large set of Ca(2+)-binding proteins that contain characteristic helix-loop-helix binding motifs that are highly conserved in sequence. Members of this family include parvalbumin and many prominent regulatory proteins such as calmodulin and troponin C. EF-hand proteins are involved in a variety of physiological processes including cell-cycle regulation, second messenger production, muscle contraction, microtubule organization and vision. RESULTS: We have determined the structures of parvalbumin mutants designed to explore the role of the last coordinating residue of the Ca(2+)-binding loop. An E101D substitution has been made in the parvalbumin EF site. The substitution decreases the Ca(2+)-binding affinity 100-fold and increases the Mg(2+)-binding affinity 10-fold. Both the Ca(2+)- and Mg(2+)-bound structures have been determined, and a structural basis has been proposed for the metal-ion-binding properties. CONCLUSIONS: The E101D mutation does not affect the Mg(2+) coordination geometry of the binding loop, but it does pull the F helix 1.1 A towards the loop. The E101D-Ca(2+) structure reveals that this mutant cannot obtain the sevenfold coordination preferred by Ca(2+), presumably because of strain limits imposed by tertiary structure. Analysis of these results relative to previously reported structural information supports a model wherein the characteristics of the last coordinating residue and the plasticity of the Ca(2+)-binding loop delimit the allowable geometries for the coordinating sphere.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-B8C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cyprinus_carpio Cyprinus carpio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B8C OCA].
+</div>
+<div class="pdbe-citations 1b8c" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Metal-ion affinity and specificity in EF-hand proteins: coordination geometry and domain plasticity in parvalbumin., Cates MS, Berry MB, Ho EL, Li Q, Potter JD, Phillips GN Jr, Structure. 1999 Oct 15;7(10):1269-78. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10545326 10545326]
+*[[Parvalbumin|Parvalbumin]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Cyprinus carpio]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Berry, M B.]]
+[[Category: Berry MB]]
-[[Category: Cates, M S.]]
+[[Category: Cates MS]]
-[[Category: Ho, E L.]]
+[[Category: Ho EL]]
-[[Category: Jr., G N.Phillips.]]
+[[Category: Li Q]]
-[[Category: Li, Q.]]
+[[Category: Phillips Jr GN]]
-[[Category: Potter, J D.]]
+[[Category: Potter JD]]
-[[Category: Calcium binding protein]]
-[[Category: Calcium-binding]]
-[[Category: Ef-hand protein]]
-[[Category: Parvalbumin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:11:48 2008''