1qx3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1qx3.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1qx3.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1qx3| PDB=1qx3 | SCENE= }}
{{STRUCTURE_1qx3| PDB=1qx3 | SCENE= }}
-
'''Conformational restrictions in the active site of unliganded human caspase-3'''
+
===Conformational restrictions in the active site of unliganded human caspase-3===
-
==Overview==
+
<!--
-
Caspases are cysteine proteases that play a critical role in the initiation and regulation of apoptosis. These enzymes act in a cascade to promote cell death through proteolytic cleavage of intracellular proteins. Since activation of apoptosis is implicated in human diseases such as cancer and neurodegenerative disorders, caspases are targets for drugs designed to modulate their action. Active caspases are heterodimeric enzymes with two symmetrically arranged active sites at opposite ends of the molecule. A number of crystal structures of caspases with peptides or proteins bound at the active sites have defined the mechanism of action of these enzymes, but molecular information about the active sites before substrate engagement has been lacking. As part of a study of peptidyl inhibitors of caspase-3, we crystallized a complex where the inhibitor did not bind in the active site. Here we present the crystal structure of the unoccupied substrate-binding site of caspase-3. No large conformational differences were apparent when this site was compared with that in enzyme-inhibitor complexes. Instead, the 1.9 A structure reveals critical side chain movements in a hydrophobic pocket in the active site. Notably, the side chain of tyrosine204 is rotated by approximately 90 degrees so that the phenol group occupies the S2 subsite in the active site. Thus, binding of substrate or inhibitors is impeded unless rotation of this side chain opens the area. The positions of these side chains may have important implications for the directed design of inhibitors of caspase-3 or caspase-7.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12833566}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12833566 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12833566}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Crystallography]]
[[Category: Crystallography]]
[[Category: Cysteine protease]]
[[Category: Cysteine protease]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:48:11 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:08:45 2008''

Revision as of 20:08, 27 July 2008

Image:1qx3.png


PDB ID 1qx3

Drag the structure with the mouse to rotate
1qx3, resolution 1.90Å ()
Gene: CASP3 OR CPP32 (Homo sapiens)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Conformational restrictions in the active site of unliganded human caspase-3

Template:ABSTRACT PUBMED 12833566

About this Structure

1QX3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Conformational restrictions in the active site of unliganded human caspase-3., Ni CZ, Li C, Wu JC, Spada AP, Ely KR, J Mol Recognit. 2003 May-Jun;16(3):121-4. PMID:12833566

Page seeded by OCA on Sun Jul 27 23:08:45 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1qx3"
Personal tools