Decamer-like conformation of a nona-peptide bound to HLA-B*3501 due to non-standard positioning of the C terminus.

doi:10.1006/jmbi.1998.2363

Back to search

Article

Decamer-like conformation of a nona-peptide bound to HLA-B*3501 due to non-standard positioning of the C terminus.

Journal of molecular biology - 15 Jan 1999

Menssen R, Orth P, Ziegler A, Saenger W

Abstract excerpt

The N and C termini of peptides presented by major histocompatibility complex (MHC) class I molecules are held within the peptide binding groove by a network of hydrogen bonds to conserved MHC residues. However, the published structure of the human allele HLA-B*3501 complexed with the nef octa-pe...

Topics

Alleles
Amino Acid Sequence
Binding Sites
Epstein-Barr Virus Nuclear Antigens
HLA-B35 Antigen
Humans
Molecular Sequence Data
Peptides
Protein Conformation
Structure-Activity Relationship

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.