3RAU
Crystal structure of the HD-PTP Bro1 domain
Summary for 3RAU
| Entry DOI | 10.2210/pdb3rau/pdb |
| Related | 3R9M |
| Descriptor | Tyrosine-protein phosphatase non-receptor type 23, ACETATE ION, 1,2-ETHANEDIOL, ... (5 entities in total) |
| Functional Keywords | bro1 domain, hydrolase |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: Q9H3S7 |
| Total number of polymer chains | 2 |
| Total formula weight | 82532.75 |
| Authors | Mu, R.L.,Jiang, J.S.,Snyder, G.,Smith, P.,Xiao, T. (deposition date: 2011-03-28, release date: 2011-09-14, Last modification date: 2023-09-13) |
| Primary citation | Sette, P.,Mu, R.,Dussupt, V.,Jiang, J.,Snyder, G.,Smith, P.,Xiao, T.S.,Bouamr, F. The Phe105 Loop of Alix Bro1 Domain Plays a Key Role in HIV-1 Release. Structure, 19:1485-1495, 2011 Cited by PubMed Abstract: Alix and cellular paralogs HD-PTP and Brox contain N-terminal Bro1 domains that bind ESCRT-III CHMP4. In contrast to HD-PTP and Brox, expression of the Bro1 domain of Alix alleviates HIV-1 release defects that result from interrupted access to ESCRT. In an attempt to elucidate this functional discrepancy, we solved the crystal structures of the Bro1 domains of HD-PTP and Brox. They revealed typical "boomerang" folds they share with the Bro1 Alix domain. However, they each contain unique structural features that may be relevant to their specific function(s). In particular, phenylalanine residue in position 105 (Phe105) of Alix belongs to a long loop that is unique to its Bro1 domain. Concurrently, mutation of Phe105 and surrounding residues at the tip of the loop compromise the function of Alix in HIV-1 budding without affecting its interactions with Gag or CHMP4. These studies identify a new functional determinant in the Bro1 domain of Alix. PubMed: 21889351DOI: 10.1016/j.str.2011.07.016 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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