Structural highlights
FunctionSPTN1_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 PubMedThe alpha-spectrin SH3 domain (Spc-SH3) is a small modular domain which has been broadly used as a model protein in folding studies and these studies have sometimes been supported by structural information obtained from the coordinates of Spc-SH3 mutants. The structure of B5/D48G, a multiple mutant designed to improve the hydrophobic core and as a consequence the protein stability, has been solved at 1 A resolution. The crystals belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a=24.79, b=37.23, c=62.95 A. This mutant also bears a D48G substitution in the distal loop and this mutation has also been reported to increase the stability of the protein by itself. The structure of the B5/D48G mutant shows a highly packed hydrophobic core and a more ordered distal loop compared with previous Spc-SH3 structures. High-resolution structure of an alpha-spectrin SH3-domain mutant with a redesigned hydrophobic core.,Camara-Artigas A, Andujar-Sanchez M, Ortiz-Salmeron E, Cuadri C, Cobos ES, Martin-Garcia JM Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Sep 1;66(Pt, 9):1023-7. Epub 2010 Aug 21. PMID:20823517[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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