1svr
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==STRUCTURE OF SEVERIN DOMAIN 2 IN SOLUTION== | ==STRUCTURE OF SEVERIN DOMAIN 2 IN SOLUTION== | ||
| - | <StructureSection load='1svr' size='340' side='right'caption='[[1svr | + | <StructureSection load='1svr' size='340' side='right'caption='[[1svr]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1svr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1svr]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1SVR FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1svr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1svr OCA], [https://pdbe.org/1svr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1svr RCSB], [https://www.ebi.ac.uk/pdbsum/1svr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1svr ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1svr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1svr OCA], [https://pdbe.org/1svr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1svr RCSB], [https://www.ebi.ac.uk/pdbsum/1svr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1svr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://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]] | ||
| Line 19: | Line 19: | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1svr ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1svr ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
| - | |||
| - | 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<ref>PMID:7897658</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1svr" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Severin|Severin]] | *[[Severin|Severin]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Dictyostelium discoideum]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Holak | + | [[Category: Holak TA]] |
| - | [[Category: Schnuchel | + | [[Category: Schnuchel A]] |
| - | + | ||
Revision as of 08:36, 1 May 2024
STRUCTURE OF SEVERIN DOMAIN 2 IN SOLUTION
| |||||||||||
