2fgh

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[[Image:2fgh.png|left|200px]]
 
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==ATP bound gelsolin==
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The line below this paragraph, containing "STRUCTURE_2fgh", creates the "Structure Box" on the page.
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<StructureSection load='2fgh' size='340' side='right'caption='[[2fgh]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2fgh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FGH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FGH FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
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<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=2fgh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fgh OCA], [http://pdbe.org/2fgh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fgh RCSB], [http://www.ebi.ac.uk/pdbsum/2fgh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fgh ProSAT]</span></td></tr>
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{{STRUCTURE_2fgh| PDB=2fgh | SCENE= }}
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/GELS_HORSE GELS_HORSE]] Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fg/2fgh_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2fgh ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Calcium activation of the actin-modifying properties of gelsolin is sensitive to ATP. Here, we show that soaking calcium-free gelsolin crystals in ATP-containing media results in ATP occupying a site that spans the two pseudosymmetrical halves of the protein. ATP binding involves numerous polar and hydrophobic contacts and is identical for the two copies of gelsolin related by non-crystallographic symmetry within the crystal. The gamma-phosphate of ATP participates in several charge-charge interactions consistent with the preference of gelsolin for ATP, as a binding partner, over ADP. In addition, disruption of the ATP-binding site through Ca2+ activation of gelsolin reveals why ATP binds more tightly to the inactive molecule, and suggests how the binding of ATP may modulate the sensitivity of gelsolin to calcium ions. Similarities between the ATP and PIP2 interactions with the C-terminal half of gelsolin are evident from their overlapping binding sites and in that both molecules bind more tightly in the absence of calcium ions. We propose a model for how PIP2 may bind to calcium-free gelsolin based on the ATP-binding site.
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===ATP bound gelsolin===
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The structure of gelsolin bound to ATP.,Urosev D, Ma Q, Tan AL, Robinson RC, Burtnick LD J Mol Biol. 2006 Mar 31;357(3):765-72. Epub 2006 Jan 25. PMID:16469333<ref>PMID:16469333</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_16469333}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2fgh" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16469333 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16469333}}
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==About this Structure==
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[[2fgh]] is a 2 chain structure of [[Gelsolin]] with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FGH OCA].
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==See Also==
==See Also==
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*[[Gelsolin]]
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*[[3D Structures of gelsolin|3D Structures of gelsolin]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:16469333</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Equus caballus]]
[[Category: Equus caballus]]
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[[Category: Burtnick, L D.]]
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[[Category: Large Structures]]
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[[Category: Ma, Q.]]
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[[Category: Burtnick, L D]]
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[[Category: Robinson, R C.]]
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[[Category: Ma, Q]]
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[[Category: Urosev, D.]]
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[[Category: Robinson, R C]]
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[[Category: Urosev, D]]
[[Category: Atp]]
[[Category: Atp]]
[[Category: Contractile protein]]
[[Category: Contractile protein]]
[[Category: Gelsolin]]
[[Category: Gelsolin]]
[[Category: Structural protein]]
[[Category: Structural protein]]

Current revision

ATP bound gelsolin

PDB ID 2fgh

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