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3m0u

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3m0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m0u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m0u RCSB], [http://www.ebi.ac.uk/pdbsum/3m0u PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3m0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m0u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m0u RCSB], [http://www.ebi.ac.uk/pdbsum/3m0u PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://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.
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 04:35, 25 December 2014

Crystal Structure of the R21D mutant of alpha-spectrin SH3 domain. Hexagonal crystal obtained in sodium formate at pH 6.5.

3m0u, resolution 1.10Å

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