Cited by 455Enzyme Structure and FunctionPeptidase Inhibition and AnalysisAmino Acid Enzymes and Metabolism

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Structure of Human Methionine Aminopeptidase-2 Complexed with Fumagillin

Liu, Shenping, Widom, Joanne, Kemp, Christopher W., Crews, Craig M., Clardy, Jon·1998·Science

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Abstract

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 Å 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.

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Refinement of Macromolecular Structures by the Maximum-Likelihood Method
Murshudov, G. N., Vagin, A. A., & Dodson, E. J. (1997) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444996012255 · Cited by 14,796
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,011
Improved methods for building protein models in electron density maps and the location of errors in these models
Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,616
Angiogenesis in cancer, vascular, rheumatoid and other disease
Folkman, J. (1995) · Nature Medicine · doi:10.1038/nm0195-27 · Cited by 7,627
LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions
Wallace, A. C., Laskowski, R. A., & Thornton, J. M. (1995) · Protein Engineering Design and Selection · doi:10.1093/protein/8.2.127 · Cited by 5,731
AMoRe: an automated package for molecular replacement
Navaza, J. (1994) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767393007597 · Cited by 4,941
Crystallographic R Factor Refinement by Molecular Dynamics
Brünger, A. T., Kuriyan, J., & Karplus, M. (1987) · Science · doi:10.1126/science.235.4787.458 · Cited by 1,950
Synthetic analogues of fumagillin that inhibit angiogenesis and suppress tumour growth
Ingber, D. E., Fujita, T., KISHIMOTO, S., Sudo, K., KANAMARU, T., Brem, H., & Folkman, J. (1990) · Nature · doi:10.1038/348555a0 · Cited by 1,301
Serine Proteases: Structure and Mechanism of Catalysis
Kraut, J. (1977) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.46.070177.001555 · Cited by 1,253
ALSCRIPT: a tool to format multiple sequence alignments
Barton, G. J. (1993) · Protein Engineering Design and Selection · doi:10.1093/protein/6.1.37 · Cited by 1,144

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J. Wang N. Quan J. Henkin Proc. Am. Assoc. Cancer Res. 39 98 (abstr.) (1998).

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Butler, M. S. (2005) · Natural Product Reports · doi:10.1039/b402985m · Cited by 496
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Vogel, C., Bashton, M., Kerrison, N. D., Chothia, C., & Teichmann, S. A. (2004) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2004.03.011 · Cited by 408
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Winter, P. M., Neubauer, A. M., Caruthers, S. D., Harris, T. D., Robertson, J. D., Williams, T. A., Schmieder, A. H., Hu, G., Allen, J. S., Lacy, E. K., et al. (2006) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.0000235724.11299.76 · Cited by 379
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Rosén, J., Lövgren, A., Kogej, T., Mureşan, S., Gottfries, J., & Backlund, A. (2008) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-008-9255-y · Cited by 100
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Authors: Liu, S., Widom, J., Kemp, C. W., Crews, C. M., & Clardy, J.
Affiliations: Cornell University (US)
Corresponding author: Clardy, Jon
ORCID: Liu, Shenping
Crews, Craig M.
Clardy, Jon
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 1998-11-13
Volume: 282
Issue: 5392
Pages: 1324-1327
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.282.5392.1324
OpenAlex: W2085785716
Cited by: 440
References: 28
Citations by year: 2026: 6 · 2025: 11 · 2024: 14 · 2023: 14 · 2022: 12 · 2021: 13 · 2020: 13 · 2019: 13 · 2018: 13 · 2017: 5 · 2016: 10 · 2015: 14 · 2014: 14 · 2013: 16 · 2012: 13
FWCI: 13.01
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Funders: National Cancer Institute (R01CA024487, CA 59021, R01CA059021, CA-24487)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Peptidase Inhibition and Analysis
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
Keywords: methionine aminopeptidase 2, fumagillin, crystal structure, enzyme-inhibitor complex, antivascular agents, anticancer agents, enzyme specificity, structure-based drug design
MeSH terms: Amino Acid Sequence, Aminopeptidases, Binding Sites, Cyclohexanes, Fatty Acids, Unsaturated, Humans, Hydrogen Bonding, Metalloendopeptidases, Models, Molecular, Molecular Sequence Data, Protein Conformation, Sesquiterpenes, Sequence Alignment, Protein Structure, Secondary, Crystallography, X-Ray

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Structure of Human Methionine Aminopeptidase-2 Complexed with Fumagillin

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