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.


1jss

From Proteopedia

Revision as of 18:51, 2 May 2008 by OCA (Talk | contribs)
Jump to: navigation, search

Template:STRUCTURE 1jss

Crystal structure of the Mus musculus cholesterol-regulated START protein 4 (StarD4).


Overview

The x-ray structure of the mouse cholesterol-regulated START protein 4 (StarD4) has been determined at 2.2-A resolution, revealing a compact alpha/beta structure related to the START domain present in the cytoplasmic C-terminal portion of human MLN64. The volume of the putative lipid-binding tunnel was estimated at 847 A(3), which is consistent with the binding of one cholesterol-size lipid molecule. Comparison of the tunnel-lining residues in StarD4 and MLN64-START permitted identification of possible lipid specificity determinants in both molecular tunnels. Homology modeling of related proteins, and comparison of the StarD4 and MLN64-START structures, showed that StarD4 is a member of a large START domain superfamily characterized by the helix-grip fold. Additional mechanistic and evolutionary studies should be facilitated by the availability of a second START domain structure from a distant relative of MLN64.

About this Structure

1JSS is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the Mus musculus cholesterol-regulated START protein 4 (StarD4) containing a StAR-related lipid transfer domain., Romanowski MJ, Soccio RE, Breslow JL, Burley SK, Proc Natl Acad Sci U S A. 2002 May 14;99(10):6949-54. PMID:12011453 Page seeded by OCA on Fri May 2 21:51:34 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools