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| | ==Calcium-free rat alpha-parvalbumin== | | ==Calcium-free rat alpha-parvalbumin== |
| - | <StructureSection load='2jww' size='340' side='right' caption='[[2jww]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2jww' size='340' side='right'caption='[[2jww]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2jww]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JWW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JWW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2jww]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JWW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JWW FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Pvalb, Pva ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr> | + | </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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jww OCA], [http://pdbe.org/2jww PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jww RCSB], [http://www.ebi.ac.uk/pdbsum/2jww PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jww ProSAT]</span></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=2jww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jww OCA], [https://pdbe.org/2jww PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jww RCSB], [https://www.ebi.ac.uk/pdbsum/2jww PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jww ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PRVA_RAT PRVA_RAT]] In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions. | + | [https://www.uniprot.org/uniprot/PRVA_RAT PRVA_RAT] In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Rattus norvegicus]] | | [[Category: Rattus norvegicus]] |
| - | [[Category: Henzl, M T]] | + | [[Category: Henzl MT]] |
| - | [[Category: Tanner, J J]] | + | [[Category: Tanner JJ]] |
| - | [[Category: Acetylation]]
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| - | [[Category: Alpha-parvalbumin]]
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| - | [[Category: Calcium-free]]
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| - | [[Category: Ef-hand protein]]
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| - | [[Category: Metal binding protein]]
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| - | [[Category: Muscle protein]]
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| - | [[Category: Phosphorylation]]
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| Structural highlights
Function
PRVA_RAT In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Mammals express two parvalbumins-an alpha isoform and a beta isoform. In rat, the alpha-parvalbumin (alpha-PV) exhibits superior divalent ion affinity. For example, the standard free energies for Ca2+ binding differ by 5.5 kcal/mol in 0.15 M KCl (pH 7.4). High-resolution structures of the Ca2+-bound proteins provide little insight into this disparity, prompting a structural analysis of the apo-proteins. A recent analysis of rat beta-PV suggested that Ca2+ removal provokes substantial conformational changes-reorientation of the C, D, and E helices; reorganization of the hydrophobic core; reduced interdomain contact; and remodeling of the AB domain. The energetic penalty attendant to reversing these changes, it was suggested, could contribute to the attenuated divalent ion-binding signature of that protein. That hypothesis is supported by data presented herein, describing the solution structure and peptide backbone dynamics of Ca2+-free rat alpha-PV. In marked contrast to rat beta-PV, the apo- and Ca2+-loaded forms of the rat alpha isoform are quite similar. Significant structural differences appear to be confined to the loop regions of the molecule. This finding implies that the alpha-PV isoform enjoys elevated divalent ion affinity because the metal ion-binding events do not require major structural rearrangement and the concomitant sacrifice of binding energy.
Solution structure of Ca2+-free rat alpha-parvalbumin.,Henzl MT, Tanner JJ Protein Sci. 2008 Mar;17(3):431-8. Epub 2008 Jan 24. PMID:18218708[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Henzl MT, Tanner JJ. Solution structure of Ca2+-free rat alpha-parvalbumin. Protein Sci. 2008 Mar;17(3):431-8. Epub 2008 Jan 24. PMID:18218708 doi:10.1110/ps.073318308
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