1rjv

<StructureSection load='1rjv' size='340' side='right'caption='[[1rjv]], [[NMR_Ensembles_of_Models | 19 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1rjv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RJV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RJV FirstGlance]. <br>

</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PVALB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>

[[https://www.uniprot.org/uniprot/PRVA_HUMAN PRVA_HUMAN]] In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions.

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== Publication Abstract from PubMed ==

In the frame of a research aimed at the detailed structural characterization of human calcium-binding proteins of the EF-hand family, the solution structure of human alpha-parvalbumin has been solved by NMR and refined with the help of substitution of the Ca(2+) ion in the EF site with the paramagnetic Dy(3+) ion. A simple (1)H-(15)N HSQC spectrum allowed the NH assignments based on the properties of Dy(3+). This allowed us to exploit pseudocontact shifts and residual dipolar couplings for solution structure refinement. The backbone and heavy atom RMSD are 0.55 +/- 0.08 and 1.02 +/- 0.08 A, respectively, and decrease to 0.39 +/- 0.05 and 0.90 +/- 0.06 A upon refinement with paramagnetism-based restraints. The RMSD for the metal itself in the EF site in the refined structure is 0.26 +/- 0.12 A. Backbone NH R(1), R(2), and NOE measured at two temperatures show the protein to be relatively rigid. The NH orientations are well determined by the paramagnetism-based restraints. This allows us to detect small but significant local structural differences with the orthologue protein from rat, whose X-ray structure is available at 2.0 A resolution. All differences are related to local changes in the amino acidic composition.

Paramagnetism-based refinement strategy for the solution structure of human alpha-parvalbumin.,Baig I, Bertini I, Del Bianco C, Gupta YK, Lee YM, Luchinat C, Quattrone A Biochemistry. 2004 May 11;43(18):5562-73. PMID:15122922<ref>PMID:15122922</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1rjv" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Human]]

[[Category: Baig, I]]

[[Category: Bertini, I]]

[[Category: Bianco, C Del]]

[[Category: Gupta, Y K]]

[[Category: Lee, Y M]]

[[Category: Luchinat, C]]

[[Category: Quattrone, A]]

[[Category: Structural proteomics in europe]]