1fq3
From Proteopedia
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| - | [[Image:1fq3.gif|left|200px]] | + | [[Image:1fq3.gif|left|200px]] |
| - | + | ||
| - | '''CRYSTAL STRUCTURE OF HUMAN GRANZYME B''' | + | {{Structure |
| + | |PDB= 1fq3 |SIZE=350|CAPTION= <scene name='initialview01'>1fq3</scene>, resolution 3.1Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF HUMAN GRANZYME B''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FQ3 is a [ | + | 1FQ3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQ3 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11209755 11209755] |
[[Category: Granzyme B]] | [[Category: Granzyme B]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: chymotrypsin-like serine proteinase]] | [[Category: chymotrypsin-like serine proteinase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:12:27 2008'' |
Revision as of 09:12, 20 March 2008
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| , resolution 3.1Å | |||||||
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| Ligands: | |||||||
| Activity: | Granzyme B, with EC number 3.4.21.79 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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