2acg

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[[Image:2acg.gif|left|200px]]
[[Image:2acg.gif|left|200px]]
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{{Structure
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|GENE= CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5755 Acanthamoeba castellanii])
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{{STRUCTURE_2acg| PDB=2acg | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2acg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2acg OCA], [http://www.ebi.ac.uk/pdbsum/2acg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2acg RCSB]</span>
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'''ACANTHAMOEBA CASTELLANII PROFILIN II'''
'''ACANTHAMOEBA CASTELLANII PROFILIN II'''
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[[Category: Magnus, K A.]]
[[Category: Magnus, K A.]]
[[Category: Pollard, T D.]]
[[Category: Pollard, T D.]]
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[[Category: actin-binding protein]]
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[[Category: Actin-binding protein]]
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[[Category: profilin]]
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[[Category: Profilin]]
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[[Category: protein binding]]
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[[Category: Protein binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:52:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:50:43 2008''
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Revision as of 15:52, 3 May 2008

Image:2acg.gif

Template:STRUCTURE 2acg

ACANTHAMOEBA CASTELLANII PROFILIN II


Overview

We determined the structures of Acanthamoeba profilin I and profilin II by x-ray crystallography at resolutions of 2.0 and 2.8 A, respectively. The polypeptide folds and the actin-binding surfaces of the amoeba profilins are very similar to those of bovine and human profilins. The electrostatic potential surfaces of the two Acanthamoeba isoforms differ. Two areas of high positive potential on the surface of profilin II are candidate binding sites for phosphatidylinositol phosphates. The proximity of these sites to the actin binding site provides an explanation for the competition between actin and lipids for binding profilin.

About this Structure

2ACG is a Single protein structure of sequence from Acanthamoeba castellanii. Full crystallographic information is available from OCA.

Reference

X-ray structures of isoforms of the actin-binding protein profilin that differ in their affinity for phosphatidylinositol phosphates., Fedorov AA, Magnus KA, Graupe MH, Lattman EE, Pollard TD, Almo SC, Proc Natl Acad Sci U S A. 1994 Aug 30;91(18):8636-40. PMID:8078936 Page seeded by OCA on Sat May 3 18:52:31 2008

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