3m0r: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 8: | Line 8: | ||
<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=3m0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m0r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m0r RCSB], [http://www.ebi.ac.uk/pdbsum/3m0r 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=3m0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m0r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m0r RCSB], [http://www.ebi.ac.uk/pdbsum/3m0r PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/SPTA2_CHICK SPTA2_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. | |||
==See Also== | ==See Also== | ||
Revision as of 19:15, 25 December 2014
Crystal Structure of the R21D mutant of alpha-spectrin SH3 domain. Crystal obtained in ammonium sulphate at pH 6.Crystal Structure of the R21D mutant of alpha-spectrin SH3 domain. Crystal obtained in ammonium sulphate at pH 6.
Structural highlights
Function[SPTA2_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. See Also |
| ||||||||||||||||||||