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Science 9 March 1990:
Vol. 247. no. 4947, pp. 1210 - 1213
DOI: 10.1126/science.2315694
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Articles

Science, Vol 247, Issue 4947, 1210-1213
Copyright © 1990 by American Association for the Advancement of Science

articles

Conserved residues make similar contacts in two repressor-operator complexes

CO Pabo, AK Aggarwal, Jordan SR, LJ Beamer, UR Obeysekare, and SC Harrison

Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205.

Comparison of a lambda repressor-operator complex and a 434 repressor-operator complex reveals that three conserved residues in the helix-turn-helix (HTH) region make similar contacts in each of the crystallographically determined structures. These conserved residues and their interactions with phosphodiester oxygens help establish a frame of reference within which other HTH residues make contacts that are critical for site-specific recognition. Such "positioning contacts" may be important conserved features within families of HTH proteins. In contrast, the structural comparisons appear to rule out any simple "recognition code" at the level of detailed side chain-base pair interactions.


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