2bss: Difference between revisions

Revision as of 04:48, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2bss.png

Template:STRUCTURE 2bss

CRYSTAL STRUCTURES AND KIR3DL1 RECOGNITION OF THREE IMMUNODOMINANT VIRAL PEPTIDES COMPLEXED TO HLA-B2705CRYSTAL STRUCTURES AND KIR3DL1 RECOGNITION OF THREE IMMUNODOMINANT VIRAL PEPTIDES COMPLEXED TO HLA-B2705

Template:ABSTRACT PUBMED 15657948

About this StructureAbout this Structure

2BSS is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures and KIR3DL1 recognition of three immunodominant viral peptides complexed to HLA-B*2705., Stewart-Jones GB, di Gleria K, Kollnberger S, McMichael AJ, Jones EY, Bowness P, Eur J Immunol. 2005 Feb;35(2):341-51. PMID:15657948

Page seeded by OCA on Tue Jul 29 04:48:31 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2bss.gif|left|200px]]
+{{Seed}}
+[[Image:2bss.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2bss|  PDB=2bss  |  SCENE=  }}
-'''CRYSTAL STRUCTURES AND KIR3DL1 RECOGNITION OF THREE IMMUNODOMINANT VIRAL PEPTIDES COMPLEXED TO HLA-B2705'''
+===CRYSTAL STRUCTURES AND KIR3DL1 RECOGNITION OF THREE IMMUNODOMINANT VIRAL PEPTIDES COMPLEXED TO HLA-B2705===
-==Overview==
+<!--
-We have solved the crystal structures of three HLA-B*2705-peptide complexes with the immunodominant viral peptides: EBV EBNA3C 258-266 (RRIYDLIEL), influenza (flu) nucleoprotein NP383-391 (SRYWAIRTR), and HIV gag 264-273 (KRWIILGLNK). Long-term non-progression during HIV infection has been associated with presentation by HLA-B*2705, and T cell recognition, of the highly immunodominant KRWIILGLNK peptide. The tight hydrogen-bonding network observed between the HLA-B*2705 B-pocket and the peptide P2 arginine guanadinium anchor explains why mutation of this residue during HIV infection results in loss of peptide binding, immune escape and progression to AIDS. Prominent, solvent-exposed structures within these peptides may participate in generating T cell responses to these immunodominant epitopes. In the HLA-B*2705 complex with flu NP383-391, the amino acid side chains of residues 4, 7 and 8 are solvent-exposed whilst in the HIV decamer, the main-chain bulges into the solvent around P7. Thus, HLA-B*2705 presents viral peptides in a range of conformations. Tetrameric complexes of HLA-B*2705 with the HIV and flu but not EBV peptides bound strongly to the killer-Ig-like receptor (KIR)3DL1. Substitution of EBV P8 glutamate to threonine allowed recognition by KIR3DL1. In the HLA-B*2705-EBV structure the P8 glutamate side chain is solvent-exposed and may inhibit KIR3DL1 binding through electrostatic forces.
+The line below this paragraph, {{ABSTRACT_PUBMED_15657948}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15657948 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15657948}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Immune system]]
 [[Category: Mhc hla-b27]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 20:44:58 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:48:31 2008''