2b4e: Difference between revisions

Revision as of 19:50, 3 May 2008

Crystal Structure of Murine Coronin-1: monoclinic form

OverviewOverview

Mammalian coronin-1 is preferentially expressed in hematopoietic cells and plays a poorly understood role in the dynamic reorganization of the actin cytoskeleton. Sequence analysis of coronin-1 revealed five WD40 repeats that were predicted to form a beta propeller. They are followed by a 130 residue extension and a 30 residue leucine zipper domain that is responsible for multimerization of the protein. Here, we present the crystal structure of murine coronin-1 without the leucine zipper at 1.75 A resolution. Coronin-1 forms a seven-bladed beta propeller composed of the five predicted WD40 repeats and two additional blades that lack any homology to the canonical WD40 motif. The C-terminal extension adopts an extended conformation, packs tightly against the bottom surface of the propeller, and is likely to be required for the structural stability of the propeller. Analysis of charged and conserved surface residues delineate possible binding sites for F-actin on the beta propeller.

About this StructureAbout this Structure

2B4E is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of murine coronin-1: a regulator of actin cytoskeletal dynamics in lymphocytes., Appleton BA, Wu P, Wiesmann C, Structure. 2006 Jan;14(1):87-96. PMID:16407068 Page seeded by OCA on Sat May 3 19:50:28 2008

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OCA

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 '''Crystal Structure of Murine Coronin-1: monoclinic form'''
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 [[Category: Wu, P.]]
 [[Category: 7-bladed beta-propeller]]
-[[Category: wd40 repeat]]
+[[Category: Wd40 repeat]]
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-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:01:15 2008''