1afo
From Proteopedia
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[[Image:1afo.gif|left|200px]] | [[Image:1afo.gif|left|200px]] | ||
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'''DIMERIC TRANSMEMBRANE DOMAIN OF HUMAN GLYCOPHORIN A, NMR, 20 STRUCTURES''' | '''DIMERIC TRANSMEMBRANE DOMAIN OF HUMAN GLYCOPHORIN A, NMR, 20 STRUCTURES''' | ||
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[[Category: Mackenzie, K R.]] | [[Category: Mackenzie, K R.]] | ||
[[Category: Prestegard, J H.]] | [[Category: Prestegard, J H.]] | ||
| - | [[Category: | + | [[Category: Human glycophorin some]] |
| - | [[Category: | + | [[Category: Integral membrane protein]] |
| - | [[Category: | + | [[Category: Membrane protein folding]] |
| - | [[Category: | + | [[Category: Transmembrane helix interaction]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:12:21 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 07:12, 2 May 2008
DIMERIC TRANSMEMBRANE DOMAIN OF HUMAN GLYCOPHORIN A, NMR, 20 STRUCTURES
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.
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 Fri May 2 10:12:21 2008
