Abstract：
:Protein-protein control recognition remains a huge challenge, and its development depends on understanding the chemical and biological mechanisms by which these interactions occur. Here we describe a protein-protein control recognition technique based on the dominant electrostatic interactions occurring between the proteins. We designed a potassium channel inhibitor, BmP05-T, that was 90.32% identical to wild-type BmP05. Negatively charged residues were translocated from the nonbinding interface to the binding interface of BmP05 inhibitor, such that BmP05-T now used BmP05 nonbinding interface as the binding interface. This switch demonstrated that nonbinding interfaces were able to control the orientation of protein binding interfaces in the process of protein-protein recognition. The novel function findings of BmP05-T peptide suggested that the control recognition technique described here had the potential for use in designing and utilizing functional proteins in many biological scenarios.
journal_name
J Proteome Resjournal_title
Journal of proteome researchauthors
Han S,Yin S,Yi H,Mouhat S,Qiu S,Cao Z,Sabatier JM,Wu Y,Li Wdoi
10.1021/pr100027ksubject
Has Abstractpub_date
2010-06-04 00:00:00pages
3118-25issue
6eissn
1535-3893issn
1535-3907journal_volume
9pub_type
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