View source for 2rmo


==Solution structure of alpha-spectrin_SH3-bergerac from Chicken==
<StructureSection load='2rmo' size='340' side='right'caption='[[2rmo]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2rmo]] 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=2RMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RMO 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=2rmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rmo OCA], [https://pdbe.org/2rmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rmo RCSB], [https://www.ebi.ac.uk/pdbsum/2rmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rmo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SPTN1_CHICK SPTN1_CHICK] Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.
== 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/rm/2rmo_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=2rmo ConSurf].
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== Publication Abstract from PubMed ==
A structural-dynamic study of one of the chimeric proteins (SHA) belonging to the SH3-Bergerac family and containing the KATANGKTYE sequence instead of the N47D48 beta-turn in the spectrin SH3 domain was carried out by high resolution NMR spectroscopy. The spatial structure of the protein was determined and its dynamics in solution was investigated on the basis of the NMR data. The elongation of the SHA polypeptide chain in comparison with the WT-SH3 original protein (by ~17%) exerts practically no effect on the general topology of the molecule. The presence of a stable beta-hairpin in the region of insertion was confirmed. This hairpin was shown to have a higher mobility in comparison with other regions of the protein.

[Study of the structure and dynamics of a chimeric variant of the SH3 domain (SHA-Bergerac) by NMR spectroscopy],Prokhorov DA, Timchenko MA, Kudrevatykh IuA, Fediukina DV, Gushchina LV, Khristoforov VS, Filimonov VV, Kutyshenko VP Bioorg Khim. 2008 Sep-Oct;34(5):645-53. PMID:19060939<ref>PMID:19060939</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 2rmo" style="background-color:#fffaf0;"></div>

==See Also==
*[[Spectrin 3D structures|Spectrin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Fedyukina DV]]
[[Category: Filimonov VV]]
[[Category: Gushchina LV]]
[[Category: Khristoforov VS]]
[[Category: Kudrevatykh YA]]
[[Category: Kutyshenko VP]]
[[Category: Prokhorov DA]]
[[Category: Timchenko MA]]