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.


1iie

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1iie.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1iie.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1iie| PDB=1iie | SCENE= }}
{{STRUCTURE_1iie| PDB=1iie | SCENE= }}
-
'''HLA-DR ANTIGENS ASSOCIATED INVARIANT CHAIN'''
+
===HLA-DR ANTIGENS ASSOCIATED INVARIANT CHAIN===
-
==Overview==
+
<!--
-
The invariant chain (Ii) plays a critical role in MHC class II antigen processing by stabilizing peptide-free class II alphabeta heterodimers in a nonameric (alphabetaIi)3 complex soon after their synthesis and directing transport of the complex from the endoplasmic reticulum to compartments where peptide loading of class II takes place. Loading progresses following Ii proteolysis and via an intermediate complex of MHC class II with an Ii-derived peptide, CLIP. CLIP is substituted by exogenous peptidic fragments in an exchange reaction catalyzed by HLA-DM. The CLIP region of Ii, roughly residues 81-104, is one of two segments shown to interact with class II HLA-DR molecules. The other segment, Ii 118-216, is C-terminal to CLIP, mediates trimerization of the ectodomain of Ii and interferes with DM/class II binding. Here we report the three-dimensional structure of this trimeric domain, determined by nuclear magnetic resonance (NMR) studies of a 27 kDa trimer of human Ii 118-192. The cylindrical shape of the molecule and the mapping of conserved residues delimit surfaces which may be important for interactions between Ii and class II molecules.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9843486}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9843486 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9843486}}
==About this Structure==
==About this Structure==
-
1IIE 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=1IIE OCA].
+
1IIE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IIE OCA].
==Reference==
==Reference==
Line 29: Line 33:
[[Category: Major histocompatibility complex]]
[[Category: Major histocompatibility complex]]
[[Category: Oligomerization]]
[[Category: Oligomerization]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:02:16 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 12:15:59 2008''

Revision as of 09:16, 1 July 2008

Image:1iie.png

Template:STRUCTURE 1iie

HLA-DR ANTIGENS ASSOCIATED INVARIANT CHAIN

Template:ABSTRACT PUBMED 9843486

About this Structure

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

Reference

Structure of a trimeric domain of the MHC class II-associated chaperonin and targeting protein Ii., Jasanoff A, Wagner G, Wiley DC, EMBO J. 1998 Dec 1;17(23):6812-8. PMID:9843486

Page seeded by OCA on Tue Jul 1 12:15:59 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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