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Sci. STKE, 12 October 1999
Vol. 1999, Issue 3, p. tw6
[DOI: 10.1126/scisignal.31999tw6]

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STKE TWIST Protein structure: Tracking Energy Through Proteins

It has frequently not been possible to use even high-resolution crystal structures of proteins to predict the residues that will be critical in some protein-protein interactions because such contacts may be buried in the molecule or at very distant sites. Lockless and Ranganathan have used structure-based alignments to look at evolutionary conservation of energetic coupling between amino acid positions in the PDZ domain family of protein-binding motifs. The patterns of energy coupling that they observed agreed with experiments in which different amino acid sites were mutated. Such studies may enable investigators to predict how energy is propagated through proteins in order for processes such as signal transduction and allosteric regulation to occur.

Lockless, S.W., and Ranganathan, R. (1999) Evolutionarily conserved pathways of energetic connectivity in protein families. Science 286: 295-299. [Abstract] [Full Text]

Citation: Protein structure: Tracking Energy Through Proteins. Sci. STKE 1999, tw6 (1999).

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