1afo

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(New page: 200px<br /> <applet load="1afo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1afo" /> '''DIMERIC TRANSMEMBRANE DOMAIN OF HUMAN GLYCO...)
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Revision as of 13:51, 12 November 2007

Image:1afo.gif

1afo

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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

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