Research article summary (published 6 Oct 1999):

Evolutionarily conserved pathways of energetic connectivity in protein families.

Full Abstract

For mapping energetic interactions in proteins, a technique was developed that uses evolutionary data for a protein family to measure statistical interactions between amino acid positions. For the PDZ domain family, this analysis predicted a set of energetically coupled positions for a binding site residue that includes unexpected long-range interactions. Mutational studies confirm these predictions, demonstrating that the statistical energy function is a good indicator of thermodynamic coupling in proteins. Sets of interacting residues form connected pathways through the protein fold that may be the basis for efficient energy conduction within proteins.

Author information

Author/s: Lockless, S W (SW); Ranganathan, R (R);

Affiliation: Howard Hughes Medical Institute and Department of Pharmacology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75235-9050, USA.

Journal and publication information

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

Journal: Science (New York, N.Y.) (Science), published in UNITED STATES. (Language: eng)

Reference: 1999-Oct; vol 286 (issue 5438) : pp 295-9

Dates: Created 1999/10/26; Completed 1999/10/26; Revised 2007/11/15;

PMID: 10514373, status: MEDLINE (last retrieved date: 2/18/2009)

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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MeSH headings (categories)

This article was linked to the MeSH Headings (categories) shown below.

Amino Acid Sequence Amino Acids - chemistry; metabolism Binding Sites Conserved Sequence Evolution, Molecular Models, Molecular Mutation Probability Protein Binding

Protein Binding Protein Conformation Protein Folding Protein Structure, Tertiary Proteins - chemistry; metabolism Recombinant Fusion Proteins - chemistry; metabolism Sequence Alignment Statistics as Topic Thermodynamics

Note: Bold headings indicate primary MeSH headings or qualifiers.

Associated Chemicals: Amino Acids (0) ; Proteins (0) ; Recombinant Fusion Proteins (0)

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