Title
Alternative protein-protein interfaces are frequent exceptions.
Abstract
The intricate molecular details of protein-protein interactions (PPIs) are crucial for function. Therefore, measuring the same interacting protein pair again, we expect the same result. This work measured the similarity in the molecular details of interaction for the same and for homologous protein pairs between different experiments. All scores analyzed suggested that different experiments often find exceptions in the interfaces of similar PPIs: up to 22% of all comparisons revealed some differences even for sequence-identical pairs of proteins. The corresponding number for pairs of close homologs reached 68%. Conversely, the interfaces differed entirely for 12-29% of all comparisons. All these estimates were calculated after redundancy reduction. The magnitude of interface differences ranged from subtle to the extreme, as illustrated by a few examples. An extreme case was a change of the interacting domains between two observations of the same biological interaction. One reason for different interfaces was the number of copies of an interaction in the same complex: the probability of observing alternative binding modes increases with the number of copies. Even after removing the special cases with alternative hetero-interfaces to the same homomer, a substantial variability remained. Our results strongly support the surprising notion that there are many alternative solutions to make the intricate molecular details of PPIs crucial for function.
Year
DOI
Venue
2012
10.1371/journal.pcbi.1002623
PLOS COMPUTATIONAL BIOLOGY
Keywords
Field
DocType
binding sites,proteins,protein protein interaction
Protein–protein interaction,Protein Interaction Networks,Biology,Protein structure comparison,Protein superfamily,Protein protein,Bioinformatics,Genetics,Protein structure
Journal
Volume
Issue
ISSN
8
8
1553-734X
Citations 
PageRank 
References 
4
0.43
15
Authors
2
Name
Order
Citations
PageRank
Tobias Hamp1553.63
Burkhard Rost279588.14