1by8: Difference between revisions

Revision as of 19:54, 30 June 2008

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File:1by8.png

Template:STRUCTURE 1by8

THE CRYSTAL STRUCTURE OF HUMAN PROCATHEPSIN KTHE CRYSTAL STRUCTURE OF HUMAN PROCATHEPSIN K

Template:ABSTRACT PUBMED 9893980

About this StructureAbout this Structure

1BY8 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of human procathepsin K., LaLonde JM, Zhao B, Janson CA, D'Alessio KJ, McQueney MS, Orsini MJ, Debouck CM, Smith WW, Biochemistry. 1999 Jan 19;38(3):862-9. PMID:9893980

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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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-'''THE CRYSTAL STRUCTURE OF HUMAN PROCATHEPSIN K'''
+===THE CRYSTAL STRUCTURE OF HUMAN PROCATHEPSIN K===
-==Overview==
+<!--
-Cathepsin K is a cysteine protease present in human osteoclasts that plays an important role in bone resorption. Cathepsin K is synthesized as an inactive proenzyme and activated under conditions of low pH. Autoproteolytic processing of the N-terminal 99 amino acid propeptide produces the active, mature form of cathepsin K. It is presumed that the activation of procathepsin K in vivo occurs in the bone resorption pit, which has a low-pH environment. We have determined the structure of human procathepsin K at 2.8 A resolution. The structure of the mature enzyme domain within procathepsin K is virtually identical to that of mature cathepsin K. The fold of the propeptide of procathepsin K is similar to that observed in procathepsins B and L despite differences in length and sequence. A portion of the propeptide occupies the active site cleft of cathepsin K. Hydrophobic interactions, salt bridges, and hydrogen-bonding interactions are observed in the structure of the propeptide and between the propeptide and the mature enzyme of procathepsin K. These interactions suggest an explanation for the stability of the proenzyme. The structure of procathepsin K contributes to an understanding of the molecular basis of inhibition by the propeptide portion of the molecule and activation of this important member of the cysteine protease family.
+The line below this paragraph, {{ABSTRACT_PUBMED_9893980}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9893980 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_9893980}}
 ==About this Structure==
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 [[Category: Zhao, B.]]
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