1VPU
NMR SOLUTION STRUCTURE OF THE HIV-1 VPU CYTOPLASMIC DOMAIN, 9 STRUCTURES
Summary for 1VPU
| Entry DOI | 10.2210/pdb1vpu/pdb |
| Descriptor | VPU PROTEIN (1 entity in total) |
| Functional Keywords | hiv, vpu, aids |
| Biological source | Human immunodeficiency virus 1 |
| Cellular location | Host membrane; Single-pass type I membrane protein (By similarity): P19554 |
| Total number of polymer chains | 1 |
| Total formula weight | 5111.44 |
| Authors | Willbold, D.,Hoffmann, S.,Rosch, P. (deposition date: 1997-01-28, release date: 1997-05-15, Last modification date: 2024-05-22) |
| Primary citation | Willbold, D.,Hoffmann, S.,Rosch, P. Secondary structure and tertiary fold of the human immunodeficiency virus protein U (Vpu) cytoplasmic domain in solution. Eur.J.Biochem., 245:581-588, 1997 Cited by PubMed Abstract: The human immunodeficiency virus type 1 Vpu protein enhances virus particle release from infected cells, decreases the tendency of syncytia formation and induces degradation of human CD4 receptor. It is known that the cytoplasmic part of Vpu is responsible for direct interaction to and degradation of CD4. The tertiary fold of the Vpu cytoplasmic domain in aqueous solution was determined employing NMR spectroscopy and molecular-dynamics simulated-annealing protocols. We found a very well defined amphipathic alpha-helix in the membrane proximal part (40-50), a less well defined helix (60-68), and a short alpha-helix at the C-terminus (75-79). We further determined the overall tertiary structure based on long-range nuclear Overhauser enhancement effects. Correlation of results from mutation experiments of Vpu and the structure data is discussed. PubMed: 9182993DOI: 10.1111/j.1432-1033.1997.t01-1-00581.x PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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