1iau
From Proteopedia
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|PDB= 1iau |SIZE=350|CAPTION= <scene name='initialview01'>1iau</scene>, resolution 2.0Å | |PDB= 1iau |SIZE=350|CAPTION= <scene name='initialview01'>1iau</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=ASA:ASPARTIC+ALDEHYDE'>ASA</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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] | + | |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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1fq3|1FQ3]], [[1fi8|1FI8]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iau OCA], [http://www.ebi.ac.uk/pdbsum/1iau PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1iau RCSB]</span> | ||
}} | }} | ||
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[[Category: Thornberry, N A.]] | [[Category: Thornberry, N A.]] | ||
[[Category: Willoughby, C A.]] | [[Category: Willoughby, C A.]] | ||
| - | [[Category: ACE]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: ZN]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:17:06 2008'' |
Revision as of 18:17, 30 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , , | ||||||
| Activity: | Granzyme B, with EC number 3.4.21.79 | ||||||
| Related: | 1FQ3, 1FI8
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN GRANZYME B IN COMPLEX WITH AC-IEPD-CHO
Overview
BACKGROUND: Granzyme B, one of the most abundant granzymes in cytotoxic T-lymphocyte (CTL) granules, and members of the caspase (cysteine aspartyl proteinases) family have a unique cleavage specificity for aspartic acid in P1 and play critical roles in the biochemical events that culminate in cell death. RESULTS: We have determined the three-dimensional structure of the complex of the human granzyme B with a potent tetrapeptide aldehyde inhibitor. The Asp-specific S1 subsite of human granzyme B is significantly larger and less charged than the corresponding Asp-specific site in the apoptosis-promoting caspases, and also larger than the corresponding subsite in rat granzyme B. CONCLUSIONS: The above differences account for the variation in substrate specificity among granzyme B, other serine proteases and the caspases, and enable the design of specific inhibitors that can probe the physiological functions of these proteins and the disease states with which they are associated.
About this Structure
1IAU is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of human granzyme B compared to caspase-3, key mediators of cell death with cleavage specificity for aspartic acid in P1., Rotonda J, Garcia-Calvo M, Bull HG, Geissler WM, McKeever BM, Willoughby CA, Thornberry NA, Becker JW, Chem Biol. 2001 Apr;8(4):357-68. PMID:11325591
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