We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1cte

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1cte.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1cte.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1cte| PDB=1cte | SCENE= }}
{{STRUCTURE_1cte| PDB=1cte | SCENE= }}
-
'''CRYSTAL STRUCTURES OF RECOMBINANT RAT CATHEPSIN B AND A CATHEPSIN B-INHIBITOR COMPLEX: IMPLICATIONS FOR STRUCTURE-BASED INHIBITOR DESIGN'''
+
===CRYSTAL STRUCTURES OF RECOMBINANT RAT CATHEPSIN B AND A CATHEPSIN B-INHIBITOR COMPLEX: IMPLICATIONS FOR STRUCTURE-BASED INHIBITOR DESIGN===
-
==Overview==
+
<!--
-
The lysosomal cysteine proteinase cathepsin B (EC 3.4.22.1) plays an important role in protein catabolism and has also been implicated in various disease states. The crystal structures of two forms of native recombinant rat cathepsin B have been determined. The overall folding of rat cathepsin B was shown to be very similar to that of the human liver enzyme. The structure of the native enzyme containing an underivatized active site cysteine (Cys29) showed the active enzyme conformation to be similar to that determined previously for the oxidized form. In a second structure Cys29 was derivatized with the reversible blocking reagent pyridyl disulfide. In this structure large side chain conformational changes were observed for the two key catalytic residues Cys29 and His199, demonstrating the potential flexibility of these side chains. In addition the structure of the complex between rat cathepsin B and the inhibitor benzyloxycarbonyl-Arg-Ser(O-Bzl) chloromethylketone was determined. The complex structure showed that very little conformational change occurs in the enzyme upon inhibitor binding. It also allowed visualization of the interaction between the enzyme and inhibitor. In particular the interaction between Glu245 and the P2 Arg residue was clearly demonstrated, and it was found that the benzyl group of the P1 substrate residue occupies a large hydrophobic pocket thought to represent the S'1 subsite. This may have important implications for structure-based design of cathepsin B inhibitors.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7890671}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7890671 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7890671}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Jia, Z.]]
[[Category: Jia, Z.]]
[[Category: Thiol protease]]
[[Category: Thiol protease]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:05:39 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:20:25 2008''

Revision as of 18:20, 30 June 2008

Image:1cte.png

Template:STRUCTURE 1cte

CRYSTAL STRUCTURES OF RECOMBINANT RAT CATHEPSIN B AND A CATHEPSIN B-INHIBITOR COMPLEX: IMPLICATIONS FOR STRUCTURE-BASED INHIBITOR DESIGN

Template:ABSTRACT PUBMED 7890671

About this Structure

1CTE is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Crystal structures of recombinant rat cathepsin B and a cathepsin B-inhibitor complex. Implications for structure-based inhibitor design., Jia Z, Hasnain S, Hirama T, Lee X, Mort JS, To R, Huber CP, J Biol Chem. 1995 Mar 10;270(10):5527-33. PMID:7890671

Page seeded by OCA on Mon Jun 30 21:20:25 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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