Structural highlights
Function
[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
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of an alpha-spectrin Src-homology 3 (SH3) domain mutant has been refined at 1.12 A resolution. This X-ray structure is at the highest resolution achieved so far for an SH3 domain. The structure allows the identification of a complete set of specific interactions and is useful for the elucidation of relations between structure and pH-dependent thermodynamic stability in a series of SH3 domain mutants.
Atomic resolution structure of a mutant of the spectrin SH3 domain.,Berisio R, Viguera A, Serrano L, Wilmanns M Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):337-40. PMID:11173498[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Berisio R, Viguera A, Serrano L, Wilmanns M. Atomic resolution structure of a mutant of the spectrin SH3 domain. Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):337-40. PMID:11173498
