A transmembrane helix dimer: structure and implica...[Science. 1997] - PubMed Result

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1: Science. 1997 Apr 4;276(5309):131-3. Links

A transmembrane helix dimer: structure and implications.

MacKenzie KR, Prestegard JH, Engelman DM.

Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA.

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.

PMID: 9082985 [PubMed - indexed for MEDLINE]

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Structures reported by this article

Dimeric Transmembrane Domain Of Human Glycophorin A, Nmr, 20 Structures

PDB: 1AFO

Source: Homo sapiens

Method: Nmr, 20 Structures

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