This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1icf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1icf.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1icf.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1icf| PDB=1icf | SCENE= }}
{{STRUCTURE_1icf| PDB=1icf | SCENE= }}
-
'''CRYSTAL STRUCTURE OF MHC CLASS II ASSOCIATED P41 II FRAGMENT IN COMPLEX WITH CATHEPSIN L'''
+
===CRYSTAL STRUCTURE OF MHC CLASS II ASSOCIATED P41 II FRAGMENT IN COMPLEX WITH CATHEPSIN L===
-
==Overview==
+
<!--
-
The lysosomal cysteine proteases cathepsins S and L play crucial roles in the degradation of the invariant chain during maturation of MHC class II molecules and antigen processing. The p41 form of the invariant chain includes a fragment which specifically inhibits cathepsin L but not S. The crystal structure of the p41 fragment, a homologue of the thyroglobulin type-1 domains, has been determined at 2.0 A resolution in complex with cathepsin L. The structure of the p41 fragment demonstrates a novel fold, consisting of two subdomains, each stabilized by disulfide bridges. The first subdomain is an alpha-helix-beta-strand arrangement, whereas the second subdomain has a predominantly beta-strand arrangement. The wedge shape and three-loop arrangement of the p41 fragment bound to the active site cleft of cathepsin L are reminiscent of the inhibitory edge of cystatins, thus demonstrating the first example of convergent evolution observed in cysteine protease inhibitors. However, the different fold of the p41 fragment results in additional contacts with the top of the R-domain of the enzymes, which defines the specificity-determining S2 and S1' substrate-binding sites. This enables inhibitors based on the thyroglobulin type-1 domain fold, in contrast to the rather non-selective cystatins, to exhibit specificity for their target enzymes.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10022822}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10022822 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10022822}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Mhc class ii]]
[[Category: Mhc class ii]]
[[Category: Thyroglobulin type-1 domain]]
[[Category: Thyroglobulin type-1 domain]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:50:32 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:45:23 2008''

Revision as of 07:45, 1 July 2008

Image:1icf.png

Template:STRUCTURE 1icf

CRYSTAL STRUCTURE OF MHC CLASS II ASSOCIATED P41 II FRAGMENT IN COMPLEX WITH CATHEPSIN L

Template:ABSTRACT PUBMED 10022822

About this Structure

1ICF is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S., Guncar G, Pungercic G, Klemencic I, Turk V, Turk D, EMBO J. 1999 Feb 15;18(4):793-803. PMID:10022822

Page seeded by OCA on Tue Jul 1 10:45:23 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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