Atomic contact vectors in protein-protein recognition.
The ability to analyze and compare protein-protein interactions on the structural level is critical to our understanding of various aspects of molecular recognition and the functional interplay of components of biochemical networks. In this study, we introduce atomic contact vectors (ACVs) as an intuitive way to represent the physico-chemical characteristics of a protein-protein interface as well as a way to compare interfaces to each other. We test the utility of ACVs in classification by using them to distinguish between homodimers and crystal contacts. Our results compare favorably with those reported by other authors. We then apply ACVs to mine the PDB for all known protein-protein complexes and separate transient recognition complexes from permanent oligomeric ones. Getting at the basis of this difference is important for our understanding of recognition and we achieved a success rate of 91% for distinguishing these two classes of complexes. Although accessible surface area of the interface is a major discriminating feature, we also show that there are distinct differences in the contact preferences between the two kinds of complexes. Illustrating the superiority of ACVs as a basic comparison measure over a sequence-based approach, we derive a general rule of thumb to determine whether two protein-protein interfaces are redundant. With this method, we arrive at a nonredundant set of 209 recognition complexes--the largest set reported so far.
Mintseris
Julian
J
Bioinformatics Program, Boston University, Boston, Massachusetts 02215, USA.
Weng
Zhiping
Z
D003460:Crystallization; D019281:Dimerization; D046911:Macromolecular Substances; D008958:Models, Molecular; D015394:Molecular Structure; D011485:Protein Binding; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000145:classification / Q000378:metabolism
D046911:Macromolecular Substances; D011506:Proteins