Evolutionary predictions of binding surfaces and interactions

by: Olivier Lichtarge, Mathew E Sowa

Current Opinion in Structural Biology, Vol. 12, No. 1. (1 February 2002), pp. 21-27.

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Abstract

Rapid progress in structural biology and whole-genome sequencing technology means that, for many protein families, structural and evolutionary information are readily available. Recent developments demonstrate how this information can be integrated to identify canonical determinants of protein structure and function. Among these determinants, those residues that are on protein surfaces are especially likely to form binding sites and are the logical choice for further mutational analysis and drug targeting.

@article{citeulike:2020899, abstract = {Rapid progress in structural biology and whole-genome sequencing technology means that, for many protein families, structural and evolutionary information are readily available. Recent developments demonstrate how this information can be integrated to identify canonical determinants of protein structure and function. Among these determinants, those residues that are on protein surfaces are especially likely to form binding sites and are the logical choice for further mutational analysis and drug targeting.}, author = {Lichtarge, Olivier and Sowa, Mathew E. }, citeulike-article-id = {2020899}, doi = {10.1016/S0959-440X(02)00284-1}, journal = {Current Opinion in Structural Biology}, keywords = {evolution, evolutionary, functional, interactions, protein-protein, sites, trace}, month = {February}, number = {1}, pages = {21--27}, posted-at = {2008-02-04 16:35:53}, priority = {3}, title = {Evolutionary predictions of binding surfaces and interactions}, url = {http://dx.doi.org/10.1016/S0959-440X(02)00284-1}, volume = {12}, year = {2002} }

RIS record

TY - JOUR ID - citeulike:2020899 L3 - citeulike-article-id:2020899 TI - Evolutionary predictions of binding surfaces and interactions JF - Current Opinion in Structural Biology VL - 12 IS - 1 SP - 21 EP - 27 N2 - Rapid progress in structural biology and whole-genome sequencing technology means that, for many protein families, structural and evolutionary information are readily available. Recent developments demonstrate how this information can be integrated to identify canonical determinants of protein structure and function. Among these determinants, those residues that are on protein surfaces are especially likely to form binding sites and are the logical choice for further mutational analysis and drug targeting. KW - evolution KW - evolutionary KW - functional KW - interactions KW - protein-protein KW - sites KW - trace AU - Lichtarge, Olivier AU - Sowa, Mathew PY - 2002/02/01/ UR - http://dx.doi.org/10.1016/S0959-440X(02)00284-1 ER -

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