1svr

STRUCTURE OF SEVERIN DOMAIN 2 IN SOLUTIONSTRUCTURE OF SEVERIN DOMAIN 2 IN SOLUTION

Structural highlights 1svr is a 1 chain structure with sequence from Dictyostelium discoideum. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 1 model Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SEVE_DICDI Severin blocks the ends of F-actin and causes the fragmentation and depolymerization of actin filaments in a Ca(2+) dependent manner. 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 three-dimensional structure of domain 2 of severin in aqueous solution was determined by nuclear magnetic resonance spectroscopy. Severin is a Ca(2+)-activated actin-binding protein that servers F-actin, nucleates actin assembly, and caps the fast-growing ends of actin filaments. The 114-residue domain consists of a central five-stranded beta-sheet, sandwiched between a parallel four-turn alpha-helix and, on the other face, a roughly perpendicular two-turn alpha-helix. There are two distinct binding sites for Ca2+ located near the N and C termini of the long helix. Conserved residues of the gelsolin-severin family contribute to the apolar core of domain 2 of severin, so that the overall fold of the protein is similar to those of segment 1 of gelsolin and profilins. Together with biochemical experiments, this structure helps to explain how severin interacts with actin. Structure of severin domain 2 in solution.,Schnuchel A, Wiltscheck R, Eichinger L, Schleicher M, Holak TA J Mol Biol. 1995 Mar 17;247(1):21-7. PMID:7897658 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Severin

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