1acf

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{{STRUCTURE_1acf| PDB=1acf | SCENE= }}
{{STRUCTURE_1acf| PDB=1acf | SCENE= }}
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'''ACANTHAMOEBA CASTELLANII PROFILIN IB'''
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===ACANTHAMOEBA CASTELLANII PROFILIN IB===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 8078936 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8078936}}
==About this Structure==
==About this Structure==
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[[Category: Profilin]]
[[Category: Profilin]]
[[Category: Protein binding]]
[[Category: Protein binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:34:51 2008''

Revision as of 13:34, 30 June 2008

Image:1acf.png

Template:STRUCTURE 1acf

ACANTHAMOEBA CASTELLANII PROFILIN IB

Template:ABSTRACT PUBMED 8078936

About this Structure

1ACF 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

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