1bn5
From Proteopedia
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[[Image:1bn5.gif|left|200px]] | [[Image:1bn5.gif|left|200px]] | ||
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'''HUMAN METHIONINE AMINOPEPTIDASE 2''' | '''HUMAN METHIONINE AMINOPEPTIDASE 2''' | ||
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[[Category: Liu, S.]] | [[Category: Liu, S.]] | ||
[[Category: Widom, J.]] | [[Category: Widom, J.]] | ||
- | [[Category: | + | [[Category: Hydrolase]] |
- | [[Category: | + | [[Category: Methionine aminopeptidase]] |
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Revision as of 08:43, 2 May 2008
HUMAN METHIONINE AMINOPEPTIDASE 2
Overview
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.
About this Structure
1BN5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of human methionine aminopeptidase-2 complexed with fumagillin., Liu S, Widom J, Kemp CW, Crews CM, Clardy J, Science. 1998 Nov 13;282(5392):1324-7. PMID:9812898 Page seeded by OCA on Fri May 2 11:43:18 2008