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''' | + | {{Structure |
| + | |PDB= 1afo |SIZE=350|CAPTION= <scene name='initialview01'>1afo</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''DIMERIC TRANSMEMBRANE DOMAIN OF HUMAN GLYCOPHORIN A, NMR, 20 STRUCTURES''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AFO is a [ | + | 1AFO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AFO OCA]. |
==Reference== | ==Reference== | ||
| - | A transmembrane helix dimer: structure and implications., MacKenzie KR, Prestegard JH, Engelman DM, Science. 1997 Apr 4;276(5309):131-3. PMID:[http:// | + | A transmembrane helix dimer: structure and implications., MacKenzie KR, Prestegard JH, Engelman DM, Science. 1997 Apr 4;276(5309):131-3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9082985 9082985] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Mackenzie, K R.]] | [[Category: Mackenzie, K R.]] | ||
[[Category: Prestegard, J H.]] | [[Category: Prestegard, J H.]] | ||
| - | [[Category: human glycophorin | + | [[Category: human glycophorin some]] |
[[Category: integral membrane protein]] | [[Category: integral membrane protein]] | ||
[[Category: membrane protein folding]] | [[Category: membrane protein folding]] | ||
| - | [[Category: transmembrane helix | + | [[Category: transmembrane helix interaction]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:56:50 2008'' |
Revision as of 07:56, 20 March 2008
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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
Page seeded by OCA on Thu Mar 20 09:56:50 2008
