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'''STRUCTURE OF SEVERIN DOMAIN 2 IN SOLUTION'''<br /> | '''STRUCTURE OF SEVERIN DOMAIN 2 IN SOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
The three-dimensional structure of domain 2 of severin in aqueous solution | 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== | ==About this Structure== | ||
1SVR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http:// | 1SVR is a [http://en.wikipedia.org/wiki/Single_protein 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=1SVR OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Dictyostelium discoideum]] | [[Category: Dictyostelium discoideum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Holak, T | [[Category: Holak, T A.]] | ||
[[Category: Schnuchel, A.]] | [[Category: Schnuchel, A.]] | ||
[[Category: actin-binding]] | [[Category: actin-binding]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:05:43 2008'' | ||
Revision as of 16:05, 21 February 2008
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STRUCTURE OF SEVERIN DOMAIN 2 IN SOLUTION
OverviewOverview
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 StructureAbout this Structure
1SVR is a Single protein structure of sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA.
ReferenceReference
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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