1SVR
STRUCTURE OF SEVERIN DOMAIN 2 IN SOLUTION
Summary for 1SVR
| Entry DOI | 10.2210/pdb1svr/pdb |
| Descriptor | SEVERIN (1 entity in total) |
| Functional Keywords | actin-binding |
| Biological source | Dictyostelium discoideum |
| Total number of polymer chains | 1 |
| Total formula weight | 12260.84 |
| Authors | Schnuchel, A.,Holak, T.A. (deposition date: 1994-10-12, release date: 1995-02-07, Last modification date: 2017-11-29) |
| Primary citation | Schnuchel, A.,Wiltscheck, R.,Eichinger, L.,Schleicher, M.,Holak, T.A. Structure of severin domain 2 in solution. J.Mol.Biol., 247:21-27, 1995 Cited by PubMed Abstract: 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. PubMed: 7897658DOI: 10.1006/jmbi.1994.0118 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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