1kq9
Human methionine aminopeptidase type II in complex with L-methionineHuman methionine aminopeptidase type II in complex with L-methionine
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHuman 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. Human methionine aminopeptidase type 2 in complex with L- and D-methionine.,Nonato MC, Widom J, Clardy J Bioorg Med Chem Lett. 2006 May 15;16(10):2580-3. Epub 2006 Mar 15. PMID:16540317[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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