1hne

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{{STRUCTURE_1hne| PDB=1hne | SCENE= }}
{{STRUCTURE_1hne| PDB=1hne | SCENE= }}
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'''STRUCTURE OF HUMAN NEUTROPHIL ELASTASE IN COMPLEX WITH A PEPTIDE CHLOROMETHYL KETONE INHIBITOR AT 1.84-ANGSTROMS RESOLUTION'''
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===STRUCTURE OF HUMAN NEUTROPHIL ELASTASE IN COMPLEX WITH A PEPTIDE CHLOROMETHYL KETONE INHIBITOR AT 1.84-ANGSTROMS RESOLUTION===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_2911584}}
==About this Structure==
==About this Structure==
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[[Category: Springer, J P.]]
[[Category: Springer, J P.]]
[[Category: Williams, H R.]]
[[Category: Williams, H R.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:25:58 2008''

Revision as of 05:26, 1 July 2008

Image:1hne.png

Template:STRUCTURE 1hne

STRUCTURE OF HUMAN NEUTROPHIL ELASTASE IN COMPLEX WITH A PEPTIDE CHLOROMETHYL KETONE INHIBITOR AT 1.84-ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 2911584

About this Structure

1HNE is a Single protein structure. Full crystallographic information is available from OCA.

Reference

Structure of human neutrophil elastase in complex with a peptide chloromethyl ketone inhibitor at 1.84-A resolution., Navia MA, McKeever BM, Springer JP, Lin TY, Williams HR, Fluder EM, Dorn CP, Hoogsteen K, Proc Natl Acad Sci U S A. 1989 Jan;86(1):7-11. PMID:2911584

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