1COK
STRUCTURE OF THE C-TERMINAL DOMAIN OF P73
Summary for 1COK
| Entry DOI | 10.2210/pdb1cok/pdb |
| NMR Information | BMRB: 4413 |
| Descriptor | PROTEIN (SECOND SPLICE VARIANT P73) (1 entity in total) |
| Functional Keywords | p73 sam-like domain, gene regulation |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: O15350 |
| Total number of polymer chains | 1 |
| Total formula weight | 7808.81 |
| Authors | Chi, S.-W.,Ayed, A.,Arrowsmith, C.H. (deposition date: 1999-05-28, release date: 1999-08-17, Last modification date: 2023-12-27) |
| Primary citation | Chi, S.W.,Ayed, A.,Arrowsmith, C.H. Solution structure of a conserved C-terminal domain of p73 with structural homology to the SAM domain. EMBO J., 18:4438-4445, 1999 Cited by PubMed Abstract: p73 and p63 are two recently cloned genes with homology to the tumor suppressor p53, whose protein product is a key transcriptional regulator of genes involved in cell cycle arrest and apoptosis. While all three proteins share conserved transcriptional activation, DNA-binding and oligomerization domains, p73 and p63 have an additional conserved C-terminal region. We have determined the three-dimensional solution structure of this conserved C-terminal domain of human p73. The structure reveals a small five-helix bundle with striking similarity to the SAM (sterile alpha motif) domains of two ephrin receptor tyrosine kinases. The SAM domain is a putative protein-protein interaction domain found in a variety of cytoplasmic signaling proteins and has been shown to form both homo- and hetero-oligomers. However, the SAM-like C-terminal domains of p73 and p63 are monomeric and do not interact with one another, suggesting that this domain may interact with additional, as yet uncharacterized proteins in a signaling and/or regulatory role. PubMed: 10449409DOI: 10.1093/emboj/18.16.4438 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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