1bn5: Difference between revisions

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[[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 1.8&Aring;" />
caption="1bn5, resolution 1.8&Aring;" />
'''HUMAN METHIONINE AMINOPEPTIDASE 2'''<br />
'''HUMAN METHIONINE AMINOPEPTIDASE 2'''<br />
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==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] Structure known Active Site: CO2. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BN5 OCA].  
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==
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[[Category: methionine aminopeptidase]]
[[Category: methionine aminopeptidase]]


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''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

File:1bn5.gif


1bn5, resolution 1.8Å

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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

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