Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Pocket mutations of HLA-B27 show that anchor residues act cumulatively to stabilize peptide binding.

Biochemistry - 21 Jun 1994

Parker K C, Biddison W E, Coligan J E

Abstract excerpt

Major histocompatibility complex (MHC) class I molecules bind endogenously synthesized peptides for presentation to cytotoxic T-cells. The human class I molecule HLA-B27 consists of a trimolecular complex containing the HLA-B27 heavy chain, a peptide that is usually nine amino acid residues (aa)...

Topics

Amino Acid Sequence
Drug Stability
Glutamine
HLA-B27 Antigen
Humans
Mathematics
Models, Chemical
Molecular Sequence Data
Mutation
Peptides
Structure-Activity Relationship
beta 2-Microglobulin

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 8011638
DOI: 10.1021/bi00190a029

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8011638-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

Community interpretation

Discuss the evidence

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

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Pocket mutations of HLA-B27 show that anchor residues act cumulatively to stabilize peptide binding.PMID 8011638Read ↗

Energetics and cooperativity of the hydrogen bonding and anchor interactions that bind peptides to MHC class II protein.Semantic proximity Read ↗

Sequence motifs important for peptide binding to the human MHC class I molecule, HLA-A2Semantic proximity Read ↗

Anchoring pockets in human histocompatibility complex leukocyte antigen (HLA) class I molecules: analysis of the conserved B ("45") pocket of HLA-B27.Semantic proximity Read ↗

Naturally occurring A pocket polymorphism in HLA-B*2703 increases the dependence on an accessory anchor residue at P1 for optimal binding of nonamer peptides.Semantic proximity Read ↗

Allele-specific B pocket transplant in class I major histocompatibility complex protein changes requirement for anchor residue at P2 of peptide.Semantic proximity Read ↗

Pocketcheck: updating the HLA class I peptide specificity roadmap.Semantic proximity Read ↗

Molecular modeling and design of invariant chain peptides with altered dissociation kinetics from class II MHC.Semantic proximity Read ↗

Modulation of peptide binding by HLA-B27 polymorphism in pockets A and B, and peptide specificity of B*2703.Semantic proximity Read ↗

Quantitation of peptide anchor residue contributions to class I major histocompatibility complex molecule binding.Semantic proximity Read ↗

Structural basis for the restoration of TCR recognition of an MHC allelic variant by peptide secondary anchor substitution.Semantic proximity Read ↗

HLA-B27 Subtypes Differentially Associated with Disease Exhibit Subtle Structural AlterationsSemantic proximity Read ↗

The Cys-67 residue of HLA-B27 influences cell surface stability, peptide specificity, and T-cell antigen presentation.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.