Human methionine aminopeptidase type 2 in complex with L- and D-methionine.
Article Details
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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
Drug Target Kind Organism Pharmacological Action Actions D-Methionine Methionine aminopeptidase 2 Protein Humans UnknownNot Available Details Methionine Methionine aminopeptidase 2 Protein Humans UnknownProduct ofDetails - Polypeptides
Name UniProt ID Methionine aminopeptidase 2 P50579 Details