Inhibition of thermolysin and neutral endopeptidase 24.11 by a novel glutaramide derivative: X-ray structure determination of the thermolysin-inhibitor complex

Determination of the X-ray structure of thermolysin-inhibitor complexes has proven useful in aiding our understanding of the mode of binding of inhibitors of related, physiologically important, mammalian zinc peptidases including neutral endopeptidase EC 3.4.24.11 and angiotensin-converting enzyme....

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Veröffentlicht in:	Biochemistry (Easton) 1994-01, Vol.33 (1), p.51-56
Hauptverfasser:	Holland, D. R, Barclay, P. L, Danilewicz, J. C, Matthews, B. W, James, K
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Biological and medical sciences Cardiotonic agents Cardiovascular system Cyclohexanecarboxylic Acids - chemistry Cyclohexanecarboxylic Acids - pharmacology Cyclopentanes - chemistry Cyclopentanes - pharmacology Dipeptides - chemistry Dipeptides - pharmacology Glycopeptides - chemistry Glycopeptides - pharmacology Kinetics Medical sciences Models, Molecular Molecular Sequence Data Molecular Structure Neprilysin - antagonists & inhibitors Neprilysin - chemistry Pharmacology. Drug treatments Protein Conformation Thermolysin - antagonists & inhibitors Thermolysin - chemistry Tryptophan - analogs & derivatives Tryptophan - chemistry Tryptophan - pharmacology X-Ray Diffraction - methods
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