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Article

A protein contortionist: core mutations of GB1 that induce dimerization and domain swapping.

Journal of molecular biology - 10 Oct 2003

Byeon In-Ja L, Louis John M, Gronenborn Angela M

Abstract excerpt

Immunoglobulin-binding domain B1 of streptococcal protein G (GB1), a small (56 residues), stable, single-domain protein, is one of the most extensively used model systems in the area of protein folding and design. Recently, NMR and X-ray structures of a quintuple GB1 core mutant (L5V/A26F/F30V/Y33F/A34F) that showed an unexpected, intertwined tetrameric architecture were determined. Here, we report the NMR...

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Identifiers

PMID: 14516749
DOI: 10.1016/s0022-2836(03)00928-8

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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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