1998
Structure of Human Methionine Aminopeptidase-2 Complexed with Fumagillin
Liu S, Widom J, Kemp C, Crews C, Clardy J. Structure of Human Methionine Aminopeptidase-2 Complexed with Fumagillin. Science 1998, 282: 1324-1327. PMID: 9812898, DOI: 10.1126/science.282.5392.1324.Peer-Reviewed Original ResearchConceptsStructure-based drug designMetAP-2Resolution crystal structureCovalent bondsMethionine aminopeptidase 2Active siteCrystal structurePolar interactionsDrug designThree-dimensional structureExtensive hydrophobicStructural basisMetAP-1Anticancer agentsNew blood vesselsFumagillin analoguesAdditional affinityReactive epoxidesMolecular targetsFumagillinStructureHydrophobicBondsLikely determinantsEpoxides
1997
The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2
Sin N, Meng L, Wang M, Wen J, Bornmann W, Crews C. The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 6099-6103. PMID: 9177176, PMCID: PMC21008, DOI: 10.1073/pnas.94.12.6099.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAminopeptidasesAnimalsAntibiotics, AntineoplasticBinding SitesCattleCyclohexanesFatty Acids, UnsaturatedHumansKineticsMammalsMetalloendopeptidasesMethionyl AminopeptidasesMolecular Sequence DataNeovascularization, PathologicO-(Chloroacetylcarbamoyl)fumagillolSaccharomyces cerevisiaeSequence AlignmentSequence Homology, Amino AcidSesquiterpenesConceptsMethionine aminopeptidaseMetAP-1MetAP-2Mammalian proteinsBlood vessel formationVegetative growthTNP-470New blood vessel formationPotent biological activitiesMolecular modeProteinFungal metabolitesVessel formationAnimal model studiesAminopeptidaseAnti-angiogenic compoundsDetailed pharmacological studiesBiological activityImportant targetFumagillinClinical trialsSolid tumorsPharmacological studiesNatural productsSaccharomyces