2qxg: Difference between revisions

Revision as of 08:15, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2qxg.png

Template:STRUCTURE 2qxg

Crystal Structure of Human Kallikrein 7 in Complex with Ala-Ala-Phe-chloromethylketoneCrystal Structure of Human Kallikrein 7 in Complex with Ala-Ala-Phe-chloromethylketone

Template:ABSTRACT PUBMED 17909180

About this StructureAbout this Structure

2QXG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Chymotryptic specificity determinants in the 1.0 A structure of the zinc-inhibited human tissue kallikrein 7., Debela M, Hess P, Magdolen V, Schechter NM, Steiner T, Huber R, Bode W, Goettig P, Proc Natl Acad Sci U S A. 2007 Oct 9;104(41):16086-91. Epub 2007 Oct 1. PMID:17909180

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal Structure of Human Kallikrein 7 in Complex with Ala-Ala-Phe-chloromethylketone'''
+===Crystal Structure of Human Kallikrein 7 in Complex with Ala-Ala-Phe-chloromethylketone===
-==Overview==
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-hK7 or human stratum corneum chymotryptic enzyme belongs to the human tissue kallikrein (hKs) serine proteinase family and is strongly expressed in the upper layers of the epidermis. It participates in skin desquamation but is also implicated in diverse skin diseases and is a potential biomarker of ovarian cancer. We have solved x-ray structures of recombinant active hK7 at medium and atomic resolution in the presence of the inhibitors succinyl-Ala-Ala-Pro-Phe-chloromethyl ketone and Ala-Ala-Phe-chloromethyl ketone. The most distinguishing features of hK7 are the short 70-80 loop and the unique S1 pocket, which prefers P1 Tyr residues, as shown by kinetic data. Similar to several other kallikreins, the enzyme activity is inhibited by Zn(2+) and Cu(2+) at low micromolar concentrations. Biochemical analyses of the mutants H99A and H41F confirm that only the metal-binding site at His(99) close to the catalytic triad accounts for the noncompetitive Zn(2+) inhibition type. Additionally, hK7 exhibits large positively charged surface patches, representing putative exosites for prime side substrate recognition.
+The line below this paragraph, {{ABSTRACT_PUBMED_17909180}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Serine protease]]
 [[Category: Zymogen]]
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