1svr: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1svr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SVR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SVR FirstGlance]. <br> | <table><tr><td colspan='2'>[[1svr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SVR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SVR FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1svq|1svq]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1svq|1svq]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1svr RCSB], [http://www.ebi.ac.uk/pdbsum/1svr PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1svr RCSB], [http://www.ebi.ac.uk/pdbsum/1svr PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/SEVE_DICDI SEVE_DICDI]] Severin blocks the ends of F-actin and causes the fragmentation and depolymerization of actin filaments in a Ca(2+) dependent manner. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Dictyostelium discoideum]] | [[Category: Dictyostelium discoideum]] | ||
[[Category: Holak, T A | [[Category: Holak, T A]] | ||
[[Category: Schnuchel, A | [[Category: Schnuchel, A]] | ||
[[Category: Actin-binding]] | [[Category: Actin-binding]] | ||
Revision as of 10:41, 25 December 2014
STRUCTURE OF SEVERIN DOMAIN 2 IN SOLUTIONSTRUCTURE OF SEVERIN DOMAIN 2 IN SOLUTION
Structural highlights
Function[SEVE_DICDI] Severin blocks the ends of F-actin and causes the fragmentation and depolymerization of actin filaments in a Ca(2+) dependent manner. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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