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Article

Structural and thermodynamic characterization of the DNA binding properties of a triple alanine mutant of MATalpha2.

Structure (London, England : 1993) - 1 Jul 2002

Ke Ailong, Mathias Jonathan R, Vershon Andrew K, Wolberger Cynthia

Abstract excerpt

Triply mutated MATalpha2 protein, alpha2-3A, in which all three major groove-contacting residues are mutated to alanine, is defective in binding DNA alone or in complex with Mcm1 yet binds with MATa1 with near wild-type affinity and specificity. To gain insight into this unexpected behavior, we determined the crystal structure of the a1/alpha2-3A/DNA complex. The structure shows that the triple mutation causes a...

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Identifiers

PMID: 12121651
DOI: 10.1016/s0969-2126(02)00790-6

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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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