1afo

From Proteopedia

Revision as of 09:44, 21 February 2008 by OCA (Talk | contribs)
Jump to: navigation, search
Image:1afo.gif

1afo

Drag the structure with the mouse to rotate

DIMERIC TRANSMEMBRANE DOMAIN OF HUMAN GLYCOPHORIN A, NMR, 20 STRUCTURES

Contents

Overview

The three-dimensional structure of the dimeric transmembrane domain of glycophorin A (GpA) was determined by solution nuclear magnetic resonance spectroscopy of a 40-residue peptide solubilized in aqueous detergent micelles. The GpA membrane-spanning alpha helices cross at an angle of -40 degrees and form a small but well-packed interface that lacks intermonomer hydrogen bonds. The structure provides an explanation for the previously characterized sequence dependence of GpA dimerization and demonstrates that van der Waals interactions alone can mediate stable and specific associations between transmembrane helices.

Disease

Known diseases associated with this structure: Blood group, MN OMIM:[111300], Malaria, resistance to OMIM:[111300]

About this Structure

1AFO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

A transmembrane helix dimer: structure and implications., MacKenzie KR, Prestegard JH, Engelman DM, Science. 1997 Apr 4;276(5309):131-3. PMID:9082985

Page seeded by OCA on Thu Feb 21 11:43:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1afo"
Personal tools