1bn5: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:1bn5.gif|left|200px]]<br /> | [[Image:1bn5.gif|left|200px]]<br /><applet load="1bn5" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1bn5" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="1bn5, resolution 1.8Å" /> | caption="1bn5, resolution 1.8Å" /> | ||
'''HUMAN METHIONINE AMINOPEPTIDASE 2'''<br /> | '''HUMAN METHIONINE AMINOPEPTIDASE 2'''<br /> | ||
Line 8: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
1BN5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CO and TBU as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] | 1BN5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CO and TBU as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] Known structural/functional Site: <scene name='pdbsite=CO2:Dicobalt Active Site'>CO2</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BN5 OCA]. | ||
==Reference== | ==Reference== | ||
Line 25: | Line 24: | ||
[[Category: methionine aminopeptidase]] | [[Category: methionine aminopeptidase]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 14:30:04 2007'' |
Revision as of 15:20, 18 December 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, for structure-based drug design.
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 Known structural/functional Site: . 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 Dec 18 14:30:04 2007