DSpace at KOASAS: High-resolution X-ray crystallography reveals precise binding interactions between human nonpancreatic secreted phospholipase A(2) and a highly potent inhibitor (FPL67047XX)

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College of Life Science and Bioengineering(생명과학기술대학)Dept. of Biological Sciences(생명과학과)BS-Journal Papers(저널논문)

High-resolution X-ray crystallography reveals precise binding interactions between human nonpancreatic secreted phospholipase A(2) and a highly potent inhibitor (FPL67047XX)

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Cha, SS / Lee, D / Adams, J / Kurdyla, JT / Jones, CS / Marshall, LA / Bolognese, B / AbdelMeguid, SS / Oh, Byung-Ha researcher

Publisher: AMER CHEMICAL SOC

Issue Date: 1996-09

Language: English

Article Type: Article

Keywords: TRANSITION-STATE ANALOG; COMPETITIVE INHIBITORS; VENOM PHOSPHOLIPASE-A2; LIPOLYTIC ENZYMES; CRYSTAL-STRUCTURE; SYNOVIAL-FLUID; SUBSTRATE; COMPLEX; DESIGN; DISEASES

Citation: JOURNAL OF MEDICINAL CHEMISTRY, v.39, no.20, pp.3878 - 3881

ISSN: 0022-2623

DOI: 10.1021/jm960502g

URI: http://hdl.handle.net/10203/74552

Appears in Collection: BS-Journal Papers(저널논문)

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High-resolution X-ray crystallography reveals precise binding interactions between human nonpancreatic secreted phospholipase A(2) and a highly potent inhibitor (FPL67047XX)

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