View source for 2nln


==Solution Structure of Calcium-free Rat Beta-parvalbumin==
<StructureSection load='2nln' size='340' side='right'caption='[[2nln]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2nln]] 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=2NLN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NLN 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=2nln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nln OCA], [https://pdbe.org/2nln PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nln RCSB], [https://www.ebi.ac.uk/pdbsum/2nln PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nln ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ONCO_RAT ONCO_RAT] Has some calmodulin-like activity with respect to enzyme activation and growth regulation. 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/nl/2nln_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=2nln ConSurf].
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== Publication Abstract from PubMed ==
Relative to other parvalbumin isoforms, the mammalian beta-parvalbumin (oncomodulin) displays attenuated divalent ion affinity. High-resolution structural data for the Ca(2+)-bound protein have provided little insight into the physical basis for this behavior, prompting an examination of the unliganded state. This article describes the solution structure and peptide backbone dynamics of Ca(2+)-free rat beta-parvalbumin (beta-PV). Ca(2+) removal evidently provokes significant structural alterations. Interaction between the D helix and the AB domain in the Ca(2+)-bound protein is greatly diminished in the apo-form, permitting the D helix to straighten. There is also a significant reorganization of the hydrophobic core and a concomitant remodeling of the interface between the AB and CD-EF domains. These modifications perturb the orientation of the C and D helices, and the energetic penalty associated with their reversal could contribute to the low-affinity signature of the CD site. By contrast, Ca(2+) removal causes a comparatively minor perturbation of the E and F helices, consistent with the more typical divalent ion affinity observed for the EF site. Ca(2+)-free rat beta-PV retains structural rigidity on the picosecond-nanosecond timescale. At 20 degrees C, the majority of amide vectors show no evidence for motion on timescales above 20 ps, and the average order parameter for the entire molecule is 0.92.

Solution structure of Ca2+-free rat beta-parvalbumin (oncomodulin).,Henzl MT, Tanner JJ Protein Sci. 2007 Sep;16(9):1914-26. PMID:17766386<ref>PMID:17766386</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Parvalbumin|Parvalbumin]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Henzl MT]]