5F67

An exquisitely specific PDZ/target recognition revealed by the structure of INAD PDZ3 in complex with TRP channel tail

Summary for 5F67

• Entry DOI: 10.2210/pdb5f67/pdb
• Descriptor: Inactivation-no-after-potential D protein, TRP C terminal Tail (3 entities in total)
• Functional Keywords: inad, trp, pdz, atypical, protein binding
• Biological source: Drosophila melanogaster (Fruit fly); More
• Cellular location: Cell membrane ; Peripheral membrane protein : Q24008
• Total number of polymer chains: 4
• Total formula weight: 27253.32

Authors

Ye, F.,Shang, Y.,Liu, W.,Zhang, M. (deposition date: 2015-12-05, release date: 2016-02-24, Last modification date: 2023-11-08)

Primary citation

Ye, F.,Liu, W.,Shang, Y.,Zhang, M.
An Exquisitely Specific PDZ/Target Recognition Revealed by the Structure of INAD PDZ3 in Complex with TRP Channel Tail
Structure, 24:383-391, 2016

PubMed Abstract: The vast majority of PDZ domains are known to bind to a few C-terminal tail residues of target proteins with modest binding affinities and specificities. Such promiscuous PDZ/target interactions are not compatible with highly specific physiological functions of PDZ domain proteins and their targets. Here, we report an unexpected PDZ/target binding occurring between the scaffold protein inactivation no afterpotential D (INAD) and transient receptor potential (TRP) channel in Drosophila photoreceptors. The C-terminal 15 residues of TRP are required for the specific interaction with INAD PDZ3. The INAD PDZ3/TRP peptide complex structure reveals that only the extreme C-terminal Leu of TRP binds to the canonical αB/βB groove of INAD PDZ3. The rest of the TRP peptide, by forming a β hairpin structure, binds to a surface away from the αB/βB groove of PDZ3 and contributes to the majority of the binding energy. Thus, the INAD PDZ3/TRP channel interaction is exquisitely specific and represents a new mode of PDZ/target recognitions.

PubMed: 26853938
DOI: 10.1016/j.str.2015.12.013

Experimental method

X-RAY DIFFRACTION (1.76 Å)