1ihj
From Proteopedia
(New page: 200px<br /><applet load="1ihj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ihj, resolution 1.8Å" /> '''Crystal Structure of ...) |
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| - | [[Image:1ihj.jpg|left|200px]]<br /><applet load="1ihj" size=" | + | [[Image:1ihj.jpg|left|200px]]<br /><applet load="1ihj" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ihj, resolution 1.8Å" /> | caption="1ihj, resolution 1.8Å" /> | ||
'''Crystal Structure of the N-terminal PDZ domain of InaD in complex with a NorpA C-terminal peptide'''<br /> | '''Crystal Structure of the N-terminal PDZ domain of InaD in complex with a NorpA C-terminal peptide'''<br /> | ||
==Overview== | ==Overview== | ||
| - | In Drosophila, phototransduction is mediated by G(q)-activation of | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1IHJ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Active as [http://en.wikipedia.org/wiki/Phospholipase_C Phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.3 3.1.4.3] Full crystallographic information is available from [http:// | + | 1IHJ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Active as [http://en.wikipedia.org/wiki/Phospholipase_C Phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.3 3.1.4.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IHJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Phospholipase C]] | [[Category: Phospholipase C]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Kimple, M | + | [[Category: Kimple, M E.]] |
| - | [[Category: Siderovski, D | + | [[Category: Siderovski, D P.]] |
[[Category: Sondek, J.]] | [[Category: Sondek, J.]] | ||
[[Category: intermolecular disulfide bond]] | [[Category: intermolecular disulfide bond]] | ||
[[Category: pdz domain]] | [[Category: pdz domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:57 2008'' |
Revision as of 11:11, 21 February 2008
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Crystal Structure of the N-terminal PDZ domain of InaD in complex with a NorpA C-terminal peptide
Overview
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.
About this Structure
1IHJ is a Protein complex structure of sequences from Drosophila melanogaster. Active as Phospholipase C, with EC number 3.1.4.3 Full crystallographic information is available from OCA.
Reference
Functional relevance of the disulfide-linked complex of the N-terminal PDZ domain of InaD with NorpA., Kimple ME, Siderovski DP, Sondek J, EMBO J. 2001 Aug 15;20(16):4414-22. PMID:11500369
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