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Characterization of PDZ domains ligands by a high efficiency strategy
Author(s) -
Tian Rui,
Ma Sucan,
Song Eli,
Gao Shijuan,
Gao Youhe
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a271-b
Subject(s) - pdz domain , computational biology , peptide library , two hybrid screening , ligand (biochemistry) , function (biology) , peptide , biology , chemistry , yeast , microbiology and biotechnology , genetics , biochemistry , peptide sequence , gene , receptor
Research over the past decade has revealed a large proportion of protein‐protein interactions are mediated by families of peptide‐binding domains. Therefore ligand‐ binding property characterization of domains is a valuable aspect in the studies of protein interaction. We have developed previously a systematic strategy for efficient binding property characterization of peptide‐binding domains based on high‐throughput validation screening of a specialized candidate ligand library using yeast two‐hybrid mating array. Its overall efficiency is dramatically improved compare to traditional screening, and it will be higher as the system cycles. PDZ domain family has been used to test the strategy. In the present work Veli3 PDZ and two unknown function proteins, PAR3L PDZ1and LNX4 PDZ1 domains have been characterized by screening traditional random peptide library combined with screening ligand library using yeast two‐hybrid. Several novel interactions have been discovered. The positive clones identified can be added to PDZ ligand library to increase its diversity for subsequent studies of PDZs. The results provide significant clues for modulation of these PDZ proteins interactions.