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.
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页码:295 / 299
页数:5
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