1svq: Difference between revisions
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[[Image:1svq.gif|left|200px]] | [[Image:1svq.gif|left|200px]] | ||
'''STRUCTURE OF SEVERIN DOMAIN 2 IN SOLUTION''' | {{Structure | ||
|PDB= 1svq |SIZE=350|CAPTION= <scene name='initialview01'>1svq</scene> | |||
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|LIGAND= | |||
|ACTIVITY= | |||
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'''STRUCTURE OF SEVERIN DOMAIN 2 IN SOLUTION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1SVQ is a [ | 1SVQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SVQ OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7897658 7897658] | ||
[[Category: Dictyostelium discoideum]] | [[Category: Dictyostelium discoideum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: actin-binding]] | [[Category: actin-binding]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:10:20 2008'' | ||
Revision as of 12:10, 20 March 2008
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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
1SVQ 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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