1fq3

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[[Image:1fq3.gif|left|200px]]
[[Image:1fq3.gif|left|200px]]
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{{Structure
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|PDB= 1fq3 |SIZE=350|CAPTION= <scene name='initialview01'>1fq3</scene>, resolution 3.1&Aring;
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The line below this paragraph, containing "STRUCTURE_1fq3", 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= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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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/Granzyme_B Granzyme B], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.79 3.4.21.79] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1fq3| PDB=1fq3 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fq3 OCA], [http://www.ebi.ac.uk/pdbsum/1fq3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fq3 RCSB]</span>
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'''CRYSTAL STRUCTURE OF HUMAN GRANZYME B'''
'''CRYSTAL STRUCTURE OF HUMAN GRANZYME B'''
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[[Category: Rubin, H.]]
[[Category: Rubin, H.]]
[[Category: Chymotrypsin-like serine proteinase]]
[[Category: Chymotrypsin-like serine proteinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:37:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat Apr 5 19:11:23 2008''
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Revision as of 13:37, 2 May 2008

Template:STRUCTURE 1fq3

CRYSTAL STRUCTURE OF HUMAN GRANZYME B


Overview

Granzyme B is the prototypic member of the granzymes, a family of trypsin-like serine proteinases localized in the dense cytoplasmic granules of activated natural killer cells and cytotoxic T lymphocytes. Granzyme B directly triggers apoptosis in target cells by activating the caspase pathway, and has been implicated in the etiology of rheumatoid arthritis. Human granzyme B expressed in a baculovirus system has been crystallized without inhibitor and its structure has been determined to 3.1 A resolution, after considerably improving the diffraction power of the crystals by controlled humidity changes. The granzyme B structure reveals an overall fold similar to that found in cathepsin G and human chymase. The guanidinium group of Arg226, anchored at the back of the S1-specificity pocket, can form a salt bridge with the P1-Asp side chain of a bound peptide substrate. The architecture of the substrate binding site of granzyme B appears to be designed to accommodate and cleave hexapeptides such as the sequence Ile-Glu-Thr-Asp-/Ser-Gly present in the activation site of pro-caspase-3, a proven physiological substrate of granzyme B. These granzyme B crystals, with fully accessible active sites, are well suited for soaking with small synthetic inhibitors that might be used for a treatment of chronic inflammatory disorders.

About this Structure

1FQ3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the caspase activator human granzyme B, a proteinase highly specific for an Asp-P1 residue., Estebanez-Perpina E, Fuentes-Prior P, Belorgey D, Braun M, Kiefersauer R, Maskos K, Huber R, Rubin H, Bode W, Biol Chem. 2000 Dec;381(12):1203-14. PMID:11209755 Page seeded by OCA on Fri May 2 16:37:49 2008

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