This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1acf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search

OCA (Talk | contribs)
(New page: 200px<br /><applet load="1acf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1acf, resolution 2.0&Aring;" /> '''ACANTHAMOEBA CASTELLA...)
Next diff →

Revision as of 08:38, 20 November 2007


1acf, resolution 2.0Å

Drag the structure with the mouse to rotate

ACANTHAMOEBA CASTELLANII PROFILIN IB

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

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

Page seeded by OCA on Tue Nov 20 10:45:16 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools