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Structure of Human Neutrophil Elastase in Complex With a Peptide Chloromethyl Ketone Inhibitor at 1.84-A Resolution

Structure of Human Neutrophil Elastase in Complex With a Peptide Chloromethyl Ketone Inhibitor at 1.84-A Resolution

M A Navia, B M McKeever, J P Springer, T Y Lin, H R Williams, E M Fluder, C P Dorn, K Hoogsteen

Proc Natl Acad Sci U S A. 1989 Jan;86(1):7-11.

PMID: 2911584

Abstract:

Human neutrophil elastase (HNE) has been implicated as a major contributor to tissue destruction in various disease states, including emphysema. The structure of HNE, at neutral pH, in complex with methoxysuccinyl-Ala-Ala-Pro-Ala chloromethyl ketone (MSACK), has been solved and refined to an R factor of 16.4% at 1.84-A resolution. Results are consistent with the currently accepted mechanism of peptide chloromethyl ketone inhibition of serine proteases, in that MSACK cross-links the catalytic residues His-57 and Ser-195. The structure of the HNE-MSACK complex is compared with that of porcine pancreatic elastase in complex with L-647,957, a beta-lactam inhibitor of both elastases. The distribution of positively charged residues on HNE is highly asymmetric and may play a role in its specific association with the underlying negatively charged proteoglycan matrix of the neutrophil granules in which the enzyme is stored.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP18171114	(Chloromethyl)-isopropoxy-dimethylsilane		18171-11-4	Price

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