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1svr
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1svq|1SVQ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1svr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1svr OCA], [http://www.ebi.ac.uk/pdbsum/1svr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1svr RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: actin-binding]] | [[Category: actin-binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:47:36 2008'' |
Revision as of 20:47, 30 March 2008
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| Related: | 1SVQ
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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