3P9G
Crystal structure of the TSG101 UEV domain in complex with FA459 peptide
Summary for 3P9G
| Entry DOI | 10.2210/pdb3p9g/pdb |
| Related | 3OBQ 3P9H |
| Descriptor | Tumor susceptibility gene 101 protein, Gag polyprotein (3 entities in total) |
| Functional Keywords | protein transport, ubiquitin |
| Biological source | Homo sapiens (human) More |
| Cellular location | Cytoplasm: Q99816 Matrix protein p17: Virion (By similarity): Q9YP46 |
| Total number of polymer chains | 2 |
| Total formula weight | 17585.30 |
| Authors | Hurley, J.H.,Im, Y.J. (deposition date: 2010-10-17, release date: 2011-06-29, Last modification date: 2023-12-06) |
| Primary citation | Kim, S.E.,Liu, F.,Im, Y.J.,Stephen, A.G.,Fivash, M.J.,Waheed, A.A.,Freed, E.O.,Fisher, R.J.,Hurley, J.H.,Burke, T.R. Elucidation of New Binding Interactions with the Tumor Susceptibility Gene 101 (Tsg101) Protein Using Modified HIV-1 Gag-p6 Derived Peptide Ligands. ACS Med Chem Lett, 2:337-341, 2011 Cited by PubMed Abstract: Targeting protein-protein interactions is gaining greater recognition as an attractive approach to therapeutic development. An example of this may be found with the human cellular protein encoded by the tumor susceptibility gene 101 (Tsg101), where interaction with the p6 C-terminal domain of the nascent viral Gag protein is required for HIV-1 particle budding and release. This association of Gag with Tsg101 is highly dependent on a "Pro-Thr-Ala-Pro" ("PTAP") peptide sequence within the p6 protein. Although p6-derived peptides offer potential starting points for developing Tsg101-binding inhibitors, the affinities of canonical peptides are outside the useful range (K(d) values greater than 50 μM). Reported herein are crystal structures of Tsg101 in complex with two structurally-modified PTAP-derived peptides. This data define new regions of ligand interaction not previously identified with canonical peptide sequences. This information could be highly useful in the design of Tsg101-binding antagonists. PubMed: 21643473DOI: 10.1021/ml1002579 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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