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.


1sje

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1sje.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1sje.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1sje| PDB=1sje | SCENE= }}
{{STRUCTURE_1sje| PDB=1sje | SCENE= }}
-
'''HLA-DR1 complexed with a 16 residue HIV capsid peptide bound in a hairpin conformation'''
+
===HLA-DR1 complexed with a 16 residue HIV capsid peptide bound in a hairpin conformation===
-
==Overview==
+
<!--
-
T cells generally recognize peptide antigens bound to MHC proteins through contacts with residues found within or immediately flanking the seven- to nine-residue sequence accommodated in the MHC peptide-binding groove. However, some T cells require peptide residues outside this region for activation, the structural basis for which is unknown. Here, we have investigated a HIV Gag-specific T cell clone that requires an unusually long peptide antigen for activation. The crystal structure of a minimally antigenic 16-mer bound to HLA-DR1 shows that the peptide C-terminal region bends sharply into a hairpin turn as it exits the binding site, orienting peptide residues outside the MHC-binding region in position to interact with a T cell receptor. Peptide truncation and substitution studies show that both the hairpin turn and the extreme C-terminal residues are required for T cell activation. These results demonstrate a previously unrecognized mode of MHC-peptide-T cell receptor interaction.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15331779}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15331779 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15331779}}
==About this Structure==
==About this Structure==
Line 37: Line 41:
[[Category: Peptide]]
[[Category: Peptide]]
[[Category: Superantigen]]
[[Category: Superantigen]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:46:38 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:11:40 2008''

Revision as of 01:11, 29 July 2008

Template:STRUCTURE 1sje

HLA-DR1 complexed with a 16 residue HIV capsid peptide bound in a hairpin conformation

Template:ABSTRACT PUBMED 15331779

About this Structure

1SJE is a Protein complex structure of sequences from Homo sapiens and Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

A hairpin turn in a class II MHC-bound peptide orients residues outside the binding groove for T cell recognition., Zavala-Ruiz Z, Strug I, Walker BD, Norris PJ, Stern LJ, Proc Natl Acad Sci U S A. 2004 Sep 7;101(36):13279-84. Epub 2004 Aug 26. PMID:15331779

Page seeded by OCA on Tue Jul 29 04:11:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools