1ihj: Difference between revisions

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[[Image:1ihj.jpg|left|200px]]
{{Seed}}
[[Image:1ihj.png|left|200px]]


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{{STRUCTURE_1ihj|  PDB=1ihj  |  SCENE=  }}  
{{STRUCTURE_1ihj|  PDB=1ihj  |  SCENE=  }}  


'''Crystal Structure of the N-terminal PDZ domain of InaD in complex with a NorpA C-terminal peptide'''
===Crystal Structure of the N-terminal PDZ domain of InaD in complex with a NorpA C-terminal peptide===




==Overview==
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In Drosophila, phototransduction is mediated by G(q)-activation of phospholipase C and is a well studied model system for understanding the kinetics of signal initiation, propagation and termination controlled by G proteins. The proper intracellular targeting and spatial arrangement of most proteins involved in fly phototransduction require the multi-domain scaffolding protein InaD, composed almost entirely of five PDZ domains, which independently bind various proteins including NorpA, the relevant phospho lipase C-beta isozyme. We have determined the crystal structure of the N-terminal PDZ domain of InaD bound to a peptide corresponding to the C-terminus of NorpA to 1.8 A resolution. The structure highlights an intermolecular disulfide bond necessary for high affinity interaction as determined by both in vitro and in vivo studies. Since other proteins also possess similar, cysteine-containing consensus sequences for binding PDZ domains, this disulfide-mediated 'dock-and-lock' interaction of PDZ domains with their ligands may be a relatively ubiquitous mode of coordinating signaling pathways.
The line below this paragraph, {{ABSTRACT_PUBMED_11500369}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_11500369}}


==About this Structure==
==About this Structure==
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[[Category: Intermolecular disulfide bond]]
[[Category: Intermolecular disulfide bond]]
[[Category: Pdz domain]]
[[Category: Pdz domain]]
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