2prf

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[[Image:2prf.png|left|200px]]
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==THREE DIMENSIONAL SOLUTION STRUCTURE OF ACANTHAMOEBA PROFILIN I==
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<StructureSection load='2prf' size='340' side='right' caption='[[2prf]], [[NMR_Ensembles_of_Models | 19 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2prf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Acanthamoeba_sp. Acanthamoeba sp.]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PRF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PRF FirstGlance]. <br>
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</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=2prf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2prf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2prf RCSB], [http://www.ebi.ac.uk/pdbsum/2prf PDBsum]</span></td></tr>
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<table>
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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/pr/2prf_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/chain_selection.php?pdb_ID=2ata 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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We have determined a medium resolution three-dimensional solution structure of Acanthamoeba profilin-I by multidimensional nuclear magnetic resonance spectroscopy. This 13-kD actin binding protein consists of a five stranded antiparallel beta sheet flanked by NH2- and COOH-terminal helices on one face and by a third helix and a two stranded beta sheet on the other face. Data from actin-profilin cross-linking experiments and the localization of conserved residues between profilins in different phyla indicate that actin binding occurs on the molecular face occupied by the terminal helices. The other face of the molecule contains the residues that differ between Acanthamoeba profilins-I and II and may be important in determining the difference in polyphosphoinositide binding between these isoforms. This suggests that lipids and actin bind to different faces of the molecule.
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{{STRUCTURE_2prf| PDB=2prf | SCENE= }}
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Three-dimensional solution structure of Acanthamoeba profilin-I.,Vinson VK, Archer SJ, Lattman EE, Pollard TD, Torchia DA J Cell Biol. 1993 Sep;122(6):1277-83. PMID:8397216<ref>PMID:8397216</ref>
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===THREE DIMENSIONAL SOLUTION STRUCTURE OF ACANTHAMOEBA PROFILIN I===
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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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{{ABSTRACT_PUBMED_8397216}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2prf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Acanthamoeba_sp. Acanthamoeba sp.]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PRF OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:008397216</ref><references group="xtra"/>
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[[Category: Acanthamoeba sp.]]
[[Category: Acanthamoeba sp.]]
[[Category: Archer, S J.]]
[[Category: Archer, S J.]]

Revision as of 20:04, 30 September 2014

THREE DIMENSIONAL SOLUTION STRUCTURE OF ACANTHAMOEBA PROFILIN I

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