1iie

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1iie.gif|left|200px]]
[[Image:1iie.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1iie |SIZE=350|CAPTION= <scene name='initialview01'>1iie</scene>
+
The line below this paragraph, containing "STRUCTURE_1iie", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND=
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY=
+
or leave the SCENE parameter empty for the default display.
-
|GENE= CD74 OR DHLAG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1iie| PDB=1iie | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iie FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iie OCA], [http://www.ebi.ac.uk/pdbsum/1iie PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1iie RCSB]</span>
+
-
}}
+
'''HLA-DR ANTIGENS ASSOCIATED INVARIANT CHAIN'''
'''HLA-DR ANTIGENS ASSOCIATED INVARIANT CHAIN'''
Line 28: Line 25:
[[Category: Wagner, G.]]
[[Category: Wagner, G.]]
[[Category: Wiley, D C.]]
[[Category: Wiley, D C.]]
-
[[Category: antigen processing]]
+
[[Category: Antigen processing]]
-
[[Category: chaperonin]]
+
[[Category: Chaperonin]]
-
[[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 Sun Mar 30 21:20:17 2008''
+

Revision as of 17:02, 2 May 2008

Template:STRUCTURE 1iie

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.

About this Structure

1IIE is a Single protein structure of sequence from Homo sapiens. Full crystallographic 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 Fri May 2 20:02:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools