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Article

High-resolution structure of an alpha-spectrin SH3-domain mutant with a redesigned hydrophobic core.

Acta crystallographica. Section F, Structural biology and crystallization communications - 1 Sept 2010

Cámara-Artigas Ana, Andújar-Sánchez Monserrat, Ortiz-Salmerón Emilia, Cuadri Celia, Cobos Eva S, Martin-Garcia Jose Manuel

Abstract excerpt

The alpha-spectrin SH3 domain (Spc-SH3) is a small modular domain which has been broadly used as a model protein in folding studies and these studies have sometimes been supported by structural information obtained from the coordinates of Spc-SH3 mutants. The structure of B5/D48G, a multiple mutant designed to improve the hydrophobic core and as a consequence the protein stability, has been solved at 1 A...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 20823517
DOI: 10.1107/S1744309110030095
PMCID: PMC2935218

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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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