1bn5: Difference between revisions
No edit summary |
No edit summary |
||
| Line 25: | Line 25: | ||
[[Category: methionine aminopeptidase]] | [[Category: methionine aminopeptidase]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14: | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:56:07 2007'' | ||
Revision as of 15:51, 30 October 2007
|
HUMAN METHIONINE AMINOPEPTIDASE 2
OverviewOverview
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, ... [(full description)]
About this StructureAbout this Structure
1BN5 is a [Single protein] structure of sequence from [Homo sapiens] with CO and TBU as [ligands]. Active as [Methionyl aminopeptidase], with EC number [3.4.11.18]. Structure known Active Site: CO2. Full crystallographic information is available from [OCA].
ReferenceReference
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 Tue Oct 30 14:56:07 2007