1aey
From Proteopedia
(Difference between revisions)
Line 5: | Line 5: | ||
</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=1aey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aey OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1aey RCSB], [http://www.ebi.ac.uk/pdbsum/1aey PDBsum]</span></td></tr> | </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=1aey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aey OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1aey RCSB], [http://www.ebi.ac.uk/pdbsum/1aey PDBsum]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [[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. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] |
Revision as of 07:26, 25 December 2014
ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, SOLUTION NMR, 15 STRUCTURES
|