1svr
From Proteopedia
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STRUCTURE OF SEVERIN DOMAIN 2 IN SOLUTION
Overview
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.
About this Structure
1SVR is a Single protein structure of sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA.
Reference
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
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