1FIT
FHIT (FRAGILE HISTIDINE TRIAD PROTEIN)
Summary for 1FIT
| Entry DOI | 10.2210/pdb1fit/pdb |
| Descriptor | FRAGILE HISTIDINE PROTEIN, beta-D-fructofuranose, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | fhit, fragile histidine triad protein, putative human tumor suppressor, advanced photon source, aps, hit protein family, pkci, chromosomal translocation |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 17352.27 |
| Authors | Lima, C.D.,D'Amico, K.L.,Naday, I.,Rosenbaum, G.,Westbrook, E.M.,Hendrickson, W.A. (deposition date: 1997-05-17, release date: 1997-11-19, Last modification date: 2024-10-30) |
| Primary citation | Lima, C.D.,D'Amico, K.L.,Naday, I.,Rosenbaum, G.,Westbrook, E.M.,Hendrickson, W.A. MAD analysis of FHIT, a putative human tumor suppressor from the HIT protein family. Structure, 5:763-774, 1997 Cited by PubMed Abstract: The fragile histidine triad (FHIT) protein is a member of the large and ubiquitous histidine triad (HIT) family of proteins. It is expressed from a gene located at a fragile site on human chromosome 3, which is commonly disrupted in association with certain cancers. On the basis of the genetic evidence, it has been postulated that the FHIT protein may function as a tumor suppressor, implying a role for the FHIT protein in carcinogenesis. The FHIT protein has dinucleoside polyphosphate hydrolase activity in vitro, thus suggesting that its role in vivo may involve the hydrolysis of a phosphoanhydride bond. The structural analysis of FHIT will identify critical residues involved in substrate binding and catalysis, and will provide insights into the in vivo function of HIT proteins. PubMed: 9261067DOI: 10.1016/S0969-2126(97)00231-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
Download full validation report
