1iau
From Proteopedia
(New page: 200px<br /> <applet load="1iau" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iau, resolution 2.0Å" /> '''HUMAN GRANZYME B IN ...) |
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| - | [[Image:1iau.gif|left|200px]]<br /> | + | [[Image:1iau.gif|left|200px]]<br /><applet load="1iau" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1iau" size=" | + | |
caption="1iau, resolution 2.0Å" /> | caption="1iau, resolution 2.0Å" /> | ||
'''HUMAN GRANZYME B IN COMPLEX WITH AC-IEPD-CHO'''<br /> | '''HUMAN GRANZYME B IN COMPLEX WITH AC-IEPD-CHO'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: Granzyme B, one of the most abundant granzymes in cytotoxic | + | 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== | ==About this Structure== | ||
| - | 1IAU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG, ZN and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1IAU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IAU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Becker, J | + | [[Category: Becker, J W.]] |
| - | [[Category: Bull, H | + | [[Category: Bull, H G.]] |
[[Category: Garcia-Calvo, M.]] | [[Category: Garcia-Calvo, M.]] | ||
| - | [[Category: Geissler, W | + | [[Category: Geissler, W M.]] |
| - | [[Category: McKeever, B | + | [[Category: McKeever, B M.]] |
[[Category: Rotonda, J.]] | [[Category: Rotonda, J.]] | ||
| - | [[Category: Thornberry, N | + | [[Category: Thornberry, N A.]] |
| - | [[Category: Willoughby, C | + | [[Category: Willoughby, C A.]] |
[[Category: ACE]] | [[Category: ACE]] | ||
[[Category: NAG]] | [[Category: NAG]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:09:53 2008'' |
Revision as of 11:09, 21 February 2008
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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 with , and as ligands. Active as Granzyme B, with EC number 3.4.21.79 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
Page seeded by OCA on Thu Feb 21 13:09:53 2008
Categories: Granzyme B | Homo sapiens | Single protein | Becker, J W. | Bull, H G. | Garcia-Calvo, M. | Geissler, W M. | McKeever, B M. | Rotonda, J. | Thornberry, N A. | Willoughby, C A. | ACE | NAG | ZN | Hydrolase
