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Science 11 February 1994:
Vol. 263. no. 5148, pp. 777 - 784
DOI: 10.1126/science.8303294
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Articles

Science, Vol 263, Issue 5148, 777-784
Copyright © 1994 by American Association for the Advancement of Science

articles

Coupling of local folding to site-specific binding of proteins to DNA

RS Spolar and MT Record Jr

Department of Chemistry, University of Wisconsin-Madison 53706.

Thermodynamic studies have demonstrated the central importance of a large negative heat capacity change (delta C degree assoc) in site-specific protein-DNA recognition. Dissection of the large negative delta C degree assoc and the entropy change of protein-ligand and protein-DNA complexation provide a thermodynamic signature identifying processes in which local folding is coupled to binding. Estimates of the number of residues that fold on binding obtained from this analysis agree with structural data. Structural comparisons indicate that these local folding transitions create key parts of the protein-DNA interface. The energetic implications of this "induced fit" model for DNA site recognition are considered.


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A. L. Kimzey and W. S. Dynan (1999)
J. Biol. Chem. 274, 34226-34232
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Glycine Insertion in the Hinge Region of Lactose Repressor Protein Alters DNA Binding.
C. M. Falcon and K. S. Matthews (1999)
J. Biol. Chem. 274, 30849-30857
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Thermodynamics of T cell receptor binding to peptide-MHC: Evidence for a general mechanism of molecular scanning.
J. J. Boniface, Z. Reich, D. S. Lyons, and M. M. Davis (1999)
PNAS 96, 11446-11451
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Crystal Structure of Anti-Hen Egg White Lysozyme Antibody (HyHEL-10) Fv-Antigen Complex. LOCAL STRUCTURAL CHANGES IN THE PROTEIN ANTIGEN AND WATER-MEDIATED INTERACTIONS OF FV-ANTIGEN AND LIGHT CHAIN-HEAVY CHAIN INTERFACES.
H. Kondo, M. Shiroishi, M. Matsushima, K. Tsumoto, and I. Kumagai (1999)
J. Biol. Chem. 274, 27623-27631
   Abstract »    Full Text »    PDF »


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