1q94: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:1q94.gif|left|200px]]
{{Seed}}
[[Image:1q94.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1q94|  PDB=1q94  |  SCENE=  }}  
{{STRUCTURE_1q94|  PDB=1q94  |  SCENE=  }}  


'''Structures of HLA-A*1101 in complex with immunodominant nonamer and decamer HIV-1 epitopes clearly reveal the presence of a middle anchor residue'''
===Structures of HLA-A*1101 in complex with immunodominant nonamer and decamer HIV-1 epitopes clearly reveal the presence of a middle anchor residue===




==Overview==
<!--  
HLA-A*1101 is one of the most common human class I alleles worldwide. An increased frequency of HLA-A*1101 has been observed in cohorts of female sex workers from Northern Thailand who are highly exposed to HIV-1 and yet have remained persistently seronegative. In view of this apparent association of HLA-A*1101 with resistance to acquisition of HIV-1 infection, and given the importance of eliciting strong CTL responses to control and eliminate HIV-1, we have determined the crystal structure of HLA-A*1101 complexed with two immunodominant HIV-1 CTL epitopes: the nonamer reverse transcriptase(313-321) (AIFQSSMTK) and decamer Nef(73-82) (QVPLRPMTYK) peptides. The structures confirm the presence of primary anchor residues P2-Ile/-Val and P9-/P10-Lys, and also clearly reveal the presence of secondary anchor residues P6-Ser for reverse transcriptase and P7-Met for Nef. The overall backbone conformation of both peptides is defined as two bulges that are separated by a more buried middle residue. In this study, we discuss how this topology may offer functional advantages in the selection and presentation of HIV-1 CTL epitopes by HLA-A*1101. Overall, this structural analysis permits a more accurate definition of the peptide-binding motif of HLA-A*1101, the characterization of its antigenic surface, and the correlation of molecular determinants with resistance to HIV-1 infection. These studies are relevant for the rational design of HLA-A*1101-restricted CTL epitopes with improved binding and immunological properties for the development of HIV-1 vaccines.
The line below this paragraph, {{ABSTRACT_PUBMED_15128805}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15128805 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_15128805}}


==Disease==
==Disease==
Line 29: Line 33:
[[Category: McNicholl, J M.]]
[[Category: McNicholl, J M.]]
[[Category: Immune system]]
[[Category: Immune system]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:01:18 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:56:44 2008''