1afo
From Proteopedia
(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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'''DIMERIC TRANSMEMBRANE DOMAIN OF HUMAN GLYCOPHORIN A, NMR, 20 STRUCTURES'''<br /> | '''DIMERIC TRANSMEMBRANE DOMAIN OF HUMAN GLYCOPHORIN A, NMR, 20 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of the dimeric transmembrane domain of | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AFO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1AFO is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Engelman, D | + | [[Category: Engelman, D M.]] |
| - | [[Category: Mackenzie, K | + | [[Category: Mackenzie, K R.]] |
| - | [[Category: Prestegard, J | + | [[Category: Prestegard, J H.]] |
[[Category: human glycophorin a]] | [[Category: human glycophorin a]] | ||
[[Category: integral membrane protein]] | [[Category: integral membrane protein]] | ||
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[[Category: transmembrane helix interactions]] | [[Category: transmembrane helix interactions]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:43:58 2008'' |
Revision as of 09:44, 21 February 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
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