Identification of the peptide binding motif for HLA-B44, one of the most common HLA-B alleles in the Caucasian population.

doi:10.1021/bi00032a005

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Article

Identification of the peptide binding motif for HLA-B44, one of the most common HLA-B alleles in the Caucasian population.

Biochemistry - 15 Aug 1995

DiBrino M, Parker K C, Margulies D H, Shiloach J, Turner R V, Biddison W E, Coligan J E

Abstract excerpt

Most peptides that bind to a particular MHC class I molecule share amino acid residues that are thought to physically "anchor" the peptide to polymorphic pockets within the class I binding site. Sequence analysis of endogenous peptides bound to HLA-B44 revealed two potential dominant anchor residues: Glu at P2 and Tyr, or occasionally Phe, at P9. In vitro assembly assays employing synthetic peptides and...

Topics

Alleles
Amino Acid Sequence
Base Sequence
Binding Sites
Capsid
DNA Primers
Epitopes
HLA-B Antigens
HLA-B44 Antigen
Humans
Influenza A virus

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Models, Molecular

Molecular Sequence Data

Peptides

T-Lymphocytes

Viral Nonstructural Proteins

White People

Source

Open in PubMed

Identifiers

PMID: 7543776
DOI: 10.1021/bi00032a005

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7543776-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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