Distinct Roles of Overlapping and Non-overlapping Regions of Hub Protein Interfaces in Recognition of Multiple Partners

JOURNAL OF MOLECULAR BIOLOGY

卷:411

Article

Dasgupta, Bhaskar^1,2  Nakamura, Haruki¹  Kinjo, Akira R.¹ 

[1] Osaka Univ, Inst Prot Res, Suita, Osaka 5650871, Japan

[2] JBIC, Koto Ku, Tokyo 1358073, Japan

关键词: date hub protein;    multiple ligand selection;    protein-protein interface;    buried and exposed interface residues;    side-chain conformations;   

DOI  :  10.1016/j.jmb.2011.06.027

来源: Elsevier

【 摘 要 】

Cellular functions of an organism are maintained by protein protein interactions. Those proteins that bind multiple partners asynchronously (date hub proteins) are important to make the interaction network coordinated. It is known that many date hub proteins bind different partners at overlapping (OV) interfaces. To understand how OV interfaces of date hub proteins can recognize multiple partners, we analyzed the difference between OV and non-overlapping (Non-OV) regions of interfaces involved in the binding of different partners. By using the structures of 16 date hub proteins with various interaction partners (ranging from 5 to 33), we compared buried surface area, compositions of amino acid residues and secondary structures, and side-chain orientations. It was found that buried interface residues are important for recognizing multiple partners, while exposed interface residues are important for determining specificity to a particular ligand. In addition, our analyses reveal that residue compositions in OV and Non-OV regions are different and that residues in OV region show diverse side-chain torsion angles to accommodate binding to multiple targets. (c) 2011 Elsevier Ltd. All rights reserved.

【 授权许可】

Free