7pck

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[[Image:7pck.gif|left|200px]]
[[Image:7pck.gif|left|200px]]
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{{Structure
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|PDB= 7pck |SIZE=350|CAPTION= <scene name='initialview01'>7pck</scene>, resolution 3.2&Aring;
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The line below this paragraph, containing "STRUCTURE_7pck", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_K Cathepsin K], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.38 3.4.22.38] </span>
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{{STRUCTURE_7pck| PDB=7pck | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=7pck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pck OCA], [http://www.ebi.ac.uk/pdbsum/7pck PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=7pck RCSB]</span>
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'''CRYSTAL STRUCTURE OF WILD TYPE HUMAN PROCATHEPSIN K'''
'''CRYSTAL STRUCTURE OF WILD TYPE HUMAN PROCATHEPSIN K'''
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[[Category: Menard, R.]]
[[Category: Menard, R.]]
[[Category: Sivaraman, J.]]
[[Category: Sivaraman, J.]]
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[[Category: cysteine protease]]
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[[Category: Cysteine protease]]
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[[Category: hydrolase (thiol protease)]]
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[[Category: Procathepsin k]]
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[[Category: procathepsin k]]
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[[Category: Proregion]]
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[[Category: proregion]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:44:35 2008''
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Revision as of 19:47, 4 May 2008

Template:STRUCTURE 7pck

CRYSTAL STRUCTURE OF WILD TYPE HUMAN PROCATHEPSIN K


Overview

Cathepsin K is a lysosomal cysteine protease belonging to the papain superfamily. It has been implicated as a major mediator of osteoclastic bone resorption. Wild-type human procathepsin K has been crystallized in a glycosylated and a deglycosylated form. The latter crystals diffract better, to 3.2 A resolution, and contain four molecules in the asymmetric unit. The structure was solved by molecular replacement and refined to an R-factor of 0.194. The N-terminal fragment of the proregion forms a globular domain while the C-terminal segment is extended and shows substantial flexibility. The proregion interacts with the enzyme along the substrate binding groove and along the proregion binding loop (residues Ser138-Asn156). It binds to the active site in the opposite direction to that of natural substrates. The overall binding mode of the proregion to cathepsin K is similar to that observed in cathepsin L, caricain, and cathepsin B, but there are local differences that likely contribute to the specificity of these proregions for their cognate enzymes. The main observed difference is in the position of the short helix alpha3p (67p-75p), which occupies the S' subsites. As in the other proenzymes, the proregion utilizes the S2 subsite for anchoring by placing a leucine side chain there, according to the specificity of cathepsin K toward its substrate.

About this Structure

7PCK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of wild-type human procathepsin K., Sivaraman J, Lalumiere M, Menard R, Cygler M, Protein Sci. 1999 Feb;8(2):283-90. PMID:10048321 Page seeded by OCA on Sun May 4 22:47:03 2008

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