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[[Image:1svq.gif|left|200px]]
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{{STRUCTURE_1svq|  PDB=1svq  |  SCENE=  }}
'''STRUCTURE OF SEVERIN DOMAIN 2 IN SOLUTION'''


==STRUCTURE OF SEVERIN DOMAIN 2 IN SOLUTION==
<StructureSection load='1svq' size='340' side='right'caption='[[1svq]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1svq]] 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=1SVQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SVQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=1svq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1svq OCA], [https://pdbe.org/1svq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1svq RCSB], [https://www.ebi.ac.uk/pdbsum/1svq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1svq ProSAT]</span></td></tr>
</table>
== 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sv/1svq_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1svq ConSurf].
<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.


==Overview==
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>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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].
</div>
<div class="pdbe-citations 1svq" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Severin|Severin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Dictyostelium discoideum]]
[[Category: Dictyostelium discoideum]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Holak, T A.]]
[[Category: Holak TA]]
[[Category: Schnuchel, A.]]
[[Category: Schnuchel A]]
[[Category: Actin-binding]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 09:11:38 2008''

Latest revision as of 07:37, 23 October 2024

STRUCTURE OF SEVERIN DOMAIN 2 IN SOLUTION

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