1iau

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1iau.gif|left|200px]]<br /><applet load="1iau" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1iau.gif|left|200px]]
-
caption="1iau, resolution 2.0&Aring;" />
+
 
-
'''HUMAN GRANZYME B IN COMPLEX WITH AC-IEPD-CHO'''<br />
+
{{Structure
 +
|PDB= 1iau |SIZE=350|CAPTION= <scene name='initialview01'>1iau</scene>, resolution 2.0&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</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=
 +
}}
 +
 
 +
'''HUMAN GRANZYME B IN COMPLEX WITH AC-IEPD-CHO'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==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 <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].
+
1IAU 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=1IAU OCA].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11325591 11325591]
+
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:[http://www.ncbi.nlm.nih.gov/pubmed/11325591 11325591]
[[Category: Granzyme B]]
[[Category: Granzyme B]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
Line 27: Line 36:
[[Category: hydrolase]]
[[Category: hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:09:53 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:47:51 2008''

Revision as of 09:47, 20 March 2008

Image:1iau.gif


PDB ID 1iau

Drag the structure with the mouse to rotate
, resolution 2.0Å
Ligands: , and
Activity: Granzyme B, with EC number 3.4.21.79
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

Page seeded by OCA on Thu Mar 20 11:47:51 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1iau"
Personal tools