1BN5
HUMAN METHIONINE AMINOPEPTIDASE 2
Summary for 1BN5
| Entry DOI | 10.2210/pdb1bn5/pdb |
| Descriptor | METHIONINE AMINOPEPTIDASE, COBALT (II) ION, TERTIARY-BUTYL ALCOHOL, ... (4 entities in total) |
| Functional Keywords | methionine aminopeptidase, hydrolase, aminopeptidase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 53251.66 |
| Authors | Liu, S.,Widom, J.,Kemp, C.W.,Crews, C.M.,Clardy, J.C. (deposition date: 1998-07-31, release date: 1999-07-31, Last modification date: 2024-10-09) |
| Primary citation | Liu, S.,Widom, J.,Kemp, C.W.,Crews, C.M.,Clardy, J. Structure of human methionine aminopeptidase-2 complexed with fumagillin. Science, 282:1324-1327, 1998 Cited by PubMed Abstract: The fungal metabolite fumagillin suppresses the formation of new blood vessels, and a fumagillin analog is currently in clinical trials as an anticancer agent. The molecular target of fumagillin is methionine aminopeptidase-2 (MetAP-2). A 1.8 A resolution crystal structure of free and inhibited human MetAP-2 shows a covalent bond formed between a reactive epoxide of fumagillin and histidine-231 in the active site of MetAP-2. Extensive hydrophobic and water-mediated polar interactions with other parts of fumagillin provide additional affinity. Fumagillin-based drugs inhibit MetAP-2 but not MetAP-1, and the three-dimensional structure also indicates the likely determinants of this specificity. The structural basis for fumagillin's potency and specificity forms the starting point for structure-based drug design. PubMed: 9812898DOI: 10.1126/science.282.5392.1324 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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