2kyf: Difference between revisions
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==solution structure of calcium-bound CPV3== | |||
<StructureSection load='2kyf' size='340' side='right'caption='[[2kyf]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2kyf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KYF 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=2kyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kyf OCA], [https://pdbe.org/2kyf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kyf RCSB], [https://www.ebi.ac.uk/pdbsum/2kyf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kyf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PRVU_CHICK PRVU_CHICK] Binds two calcium ions. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Birds express two beta-parvalbumin isoforms, parvalbumin 3 and avian thymic hormone (ATH). Parvalbumin 3 from chicken (CPV3) is identical to rat beta-parvalbumin (beta-PV) at 75 of 108 residues. CPV3 displays intermediate Ca(2+) affinity-higher than that of rat beta-parvalbumin, but lower than that of ATH. As in rat beta-PV, the attenuation of affinity is associated primarily with the CD site (residues 41-70), rather than the EF site (residues 80-108). Structural data for rat alpha- and beta-parvalbumins suggest that divalent ion affinity is correlated with the similarity of the unliganded and Ca(2+) -bound conformations. We herein present a comparison of the solution structures of Ca(2+) -free and Ca(2+) -bound CPV3. Although the structures are generally similar, the conformations of residues 47 to 50 differ markedly in the two protein forms. These residues are located in the C helix, proximal to the CD binding loop. In response to Ca(2+) removal, F47 experiences much greater solvent accessibility. The side-chain of R48 assumes a position between the C and D helices, adjacent to R69. Significantly, I49 adopts an interior position in the unliganded protein that allows association with the side-chain of L50. Concomitantly, the realignment of F66 and F70 facilitates their interaction with I49 and reduces their contact with residues in the N-terminal AB domain. This reorganization of the hydrophobic core, although less profound, is nevertheless reminiscent of that observed in rat beta-PV. The results lend further support to the idea that Ca(2+) affinity correlates with the structural similarity of the apo- and bound parvalbumin conformations. Proteins 2011. (c) 2010 Wiley-Liss, Inc. | |||
Solution structures of chicken parvalbumin 3 in the Ca(2+) -free and Ca(2+) -bound states.,Henzl MT, Tanner JJ, Tan A Proteins. 2011 Mar;79(3):752-64. doi: 10.1002/prot.22915. Epub 2010 Dec 3. PMID:21287610<ref>PMID:21287610</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2kyf" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Parvalbumin|Parvalbumin]] | *[[Parvalbumin|Parvalbumin]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Henzl MT]] | ||
[[Category: | [[Category: Tan A]] | ||
[[Category: | [[Category: Tanner JJ]] | ||
Latest revision as of 08:37, 15 May 2024
solution structure of calcium-bound CPV3solution structure of calcium-bound CPV3
Structural highlights
FunctionPRVU_CHICK Binds two calcium ions. Publication Abstract from PubMedBirds express two beta-parvalbumin isoforms, parvalbumin 3 and avian thymic hormone (ATH). Parvalbumin 3 from chicken (CPV3) is identical to rat beta-parvalbumin (beta-PV) at 75 of 108 residues. CPV3 displays intermediate Ca(2+) affinity-higher than that of rat beta-parvalbumin, but lower than that of ATH. As in rat beta-PV, the attenuation of affinity is associated primarily with the CD site (residues 41-70), rather than the EF site (residues 80-108). Structural data for rat alpha- and beta-parvalbumins suggest that divalent ion affinity is correlated with the similarity of the unliganded and Ca(2+) -bound conformations. We herein present a comparison of the solution structures of Ca(2+) -free and Ca(2+) -bound CPV3. Although the structures are generally similar, the conformations of residues 47 to 50 differ markedly in the two protein forms. These residues are located in the C helix, proximal to the CD binding loop. In response to Ca(2+) removal, F47 experiences much greater solvent accessibility. The side-chain of R48 assumes a position between the C and D helices, adjacent to R69. Significantly, I49 adopts an interior position in the unliganded protein that allows association with the side-chain of L50. Concomitantly, the realignment of F66 and F70 facilitates their interaction with I49 and reduces their contact with residues in the N-terminal AB domain. This reorganization of the hydrophobic core, although less profound, is nevertheless reminiscent of that observed in rat beta-PV. The results lend further support to the idea that Ca(2+) affinity correlates with the structural similarity of the apo- and bound parvalbumin conformations. Proteins 2011. (c) 2010 Wiley-Liss, Inc. Solution structures of chicken parvalbumin 3 in the Ca(2+) -free and Ca(2+) -bound states.,Henzl MT, Tanner JJ, Tan A Proteins. 2011 Mar;79(3):752-64. doi: 10.1002/prot.22915. Epub 2010 Dec 3. PMID:21287610[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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