Human methionine aminopeptidase type 2 in complex with L- and D-methionine.

Article Details

Citation

Nonato MC, Widom J, Clardy J

Human methionine aminopeptidase type 2 in complex with L- and D-methionine.

Bioorg Med Chem Lett. 2006 May 15;16(10):2580-3. Epub 2006 Mar 15.

PubMed ID
16540317 [ View in PubMed
]
Abstract

Human methionine aminopeptidase type 2 (hMetAP-2) was identified as the molecular target of anti-angiogenic agents such as fumagillin and its analogues. We describe here the crystal structure of hMetAP-2 in complex with l-methionine and d-methionine at 1.9 and 2.0A resolution, respectively. The comparison of the structure of the two complexes establishes the basis of enantiomer discrimination and provides some considerations for the design of selective MetAP-2 inhibitors.

DrugBank Data that Cites this Article

Drug Targets
DrugTargetKindOrganismPharmacological ActionActions
D-MethionineMethionine aminopeptidase 2ProteinHumans
Unknown
Not AvailableDetails
MethionineMethionine aminopeptidase 2ProteinHumans
Unknown
Product of
Details
Polypeptides
NameUniProt ID
Methionine aminopeptidase 2P50579Details