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Homology Among DNA-binding Proteins Suggests Use of a Conserved Super-secondary Structure

Overview
Journal Nature
Specialty Science
Date 1982 Jul 29
PMID 6896364
Citations 149
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Abstract

The amino acid sequences of the repressor and cro proteins of phages lambda, 434 and P22 are homologous, especially in a region in which repressor and lambda cro have a similar alpha-helix-turn-alpha-helix secondary structure. Model-building studies indicate that this structure is important in DNA binding, and we suggest it may be a common feature of many DNa-binding proteins.

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