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Article

Coiled-coil destabilizing residues in the group A Streptococcus M1 protein are required for functional interaction.

Proceedings of the National Academy of Sciences of the United States of America - 23 Aug 2016

Stewart Chelsea M, Buffalo Cosmo Z, Valderrama J Andrés, Henningham Anna, Cole Jason N, Nizet Victor, Ghosh Partho

Abstract excerpt

The sequences of M proteins, the major surface-associated virulence factors of the widespread bacterial pathogen group A Streptococcus, are antigenically variable but have in common a strong propensity to form coiled coils. Paradoxically, these sequences are also replete with coiled-coil destabilizing residues. These features are evident in the irregular coiled-coil structure and thermal instability of M...

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Share to Amino Acids
Share to Antigens, Bacterial

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Bacterial Outer Membrane Proteins

Share to Fibrinogen

Share to Protein Conformation, alpha-Helical

Share to Protein Interaction Domains and Motifs

Share to Streptococcus pyogenes

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Source

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Identifiers

PMID: 27512043
DOI: 10.1073/pnas.1606160113
PMCID: PMC5003295

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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