1AFO
DIMERIC TRANSMEMBRANE DOMAIN OF HUMAN GLYCOPHORIN A, NMR, 20 STRUCTURES
Summary for 1AFO
| Entry DOI | 10.2210/pdb1afo/pdb |
| Descriptor | GLYCOPHORIN A (1 entity in total) |
| Functional Keywords | integral membrane protein, human glycophorin a, transmembrane helix interactions, membrane protein folding |
| Biological source | Homo sapiens (human) |
| Cellular location | Cell membrane; Single-pass type I membrane protein: P02724 |
| Total number of polymer chains | 2 |
| Total formula weight | 8908.83 |
| Authors | Mackenzie, K.R.,Prestegard, J.H.,Engelman, D.M. (deposition date: 1997-03-11, release date: 1997-09-17, Last modification date: 2024-05-22) |
| Primary citation | MacKenzie, K.R.,Prestegard, J.H.,Engelman, D.M. A transmembrane helix dimer: structure and implications. Science, 276:131-133, 1997 Cited by PubMed Abstract: 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. PubMed: 9082985DOI: 10.1126/science.276.5309.131 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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