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Article

Core mutations switch monomeric protein GB1 into an intertwined tetramer.

Nature structural biology - 1 Nov 2002

Kirsten Frank M, Dyda Fred, Dobrodumov Anatoliy, Gronenborn Angela M

Abstract excerpt

The structure of a mutant immunoglobulin-binding B1 domain of streptococcal protein G (GB1), which comprises five conservative changes in hydrophobic core residues, was determined by NMR spectroscopy and X-ray crystallography. The oligomeric state and quaternary structure of the mutant protein are drastically changed from the wild type protein. The mutant structure consists of a symmetric tetramer, with...

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Identifiers

PMID: 12379842
DOI: 10.1038/nsb854

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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