5EH6
Crystal Structure of the Glycophorin A Transmembrane Monomer in Lipidic Cubic Phase
Summary for 5EH6
| Entry DOI | 10.2210/pdb5eh6/pdb |
| Related | 5EH4 |
| Descriptor | Glycophorin-A (1 entity in total) |
| Functional Keywords | receptor, lipidic cubic phase, peptides, transmembrane, membrane protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 3292.05 |
| Authors | Call, M.J.,Call, M.E.,Trenker, R. (deposition date: 2015-10-28, release date: 2015-12-23, Last modification date: 2023-09-27) |
| Primary citation | Trenker, R.,Call, M.E.,Call, M.J. Crystal Structure of the Glycophorin A Transmembrane Dimer in Lipidic Cubic Phase. J.Am.Chem.Soc., 137:15676-15679, 2015 Cited by PubMed Abstract: The mechanisms of assembly and function for many important type I/II (single-pass) transmembrane (TM) receptors are proposed to involve the formation and/or alteration of specific interfaces among their membrane-embedded α-helical TM domains. The application of lipidic cubic phase (LCP) bilayer media for crystallization of single-α-helical TM complexes has the potential to provide valuable structural and mechanistic insights into many such systems. However, the fidelity of the interfaces observed in crowded crystalline arrays has been difficult to establish from the very limited number of such structures determined using X-ray diffraction data. Here we examine this issue using the glycophorin A (GpA) model system, whose homodimeric TM helix interface has been characterized by solution and solid-state NMR and biochemical techniques but never crystallographically. We report that a GpA-TM peptide readily crystallized in a monoolein cubic phase bilayer, yielding a dimeric α-helical structure that is in excellent agreement with previously reported NMR measurements made in several different types of host media. These results provide compelling support for the wider application of LCP techniques to enable X-ray crystallographic analysis of single-pass TM interactions. PubMed: 26642914DOI: 10.1021/jacs.5b11354 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.918 Å) |
Structure validation
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