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==THREE DIMENSIONAL SOLUTION STRUCTURE OF ACANTHAMOEBA PROFILIN I==
==THREE DIMENSIONAL SOLUTION STRUCTURE OF ACANTHAMOEBA PROFILIN I==
<StructureSection load='2prf' size='340' side='right'caption='[[2prf]], [[NMR_Ensembles_of_Models | 19 NMR models]]' scene=''>
<StructureSection load='2prf' size='340' side='right'caption='[[2prf]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>[[2prf]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2PRF FirstGlance]. <br>
</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=2prf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2prf OCA], [http://pdbe.org/2prf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2prf RCSB], [http://www.ebi.ac.uk/pdbsum/2prf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2prf ProSAT]</span></td></tr>
</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=2prf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2prf OCA], [https://pdbe.org/2prf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2prf RCSB], [https://www.ebi.ac.uk/pdbsum/2prf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2prf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PRO1A_ACACA PRO1A_ACACA] Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=2prf 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=2prf ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2prf" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Profilin 3D Structures|Profilin 3D Structures]]
*[[Profilin 3D Structures|Profilin 3D Structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Acanthamoeba sp]]
[[Category: Acanthamoeba sp]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Archer, S J]]
[[Category: Archer SJ]]
[[Category: Lattman, E E]]
[[Category: Lattman EE]]
[[Category: Pollard, T D]]
[[Category: Pollard TD]]
[[Category: Torchia, D A]]
[[Category: Torchia DA]]
[[Category: Vinson, V K]]
[[Category: Vinson VK]]
[[Category: Actin-binding]]

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