View source for 2kyc


==solution structure of Ca-free chicken parvalbumin 3 (CPV3)==
<StructureSection load='2kyc' size='340' side='right'caption='[[2kyc]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2kyc]] 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=2KYC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KYC 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=2kyc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kyc OCA], [https://pdbe.org/2kyc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kyc RCSB], [https://www.ebi.ac.uk/pdbsum/2kyc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kyc 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2kyc" style="background-color:#fffaf0;"></div>

==See Also==
*[[Parvalbumin|Parvalbumin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Henzl NT]]
[[Category: Tan A]]
[[Category: Tanner JJ]]