Evolutionarily conserved pathways of energetic connectivity in protein families

被引:1068
作者
Lockless, SW
Ranganathan, R
机构
[1] Univ Texas, SW Med Ctr, Howard Hughes Med Inst, Dallas, TX 75235 USA
[2] Univ Texas, SW Med Ctr, Dept Pharmacol, Dallas, TX 75235 USA
关键词
D O I
10.1126/science.286.5438.295
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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 intracting residues form connected pathways through the protein fold that may be the basis for efficient energy conduction within proteins.
引用
收藏
页码:295 / 299
页数:5
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