2dc2
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Revision as of 19:24, 12 November 2007
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Solution Structure of PDZ Domain
Contents |
Overview
GOPC (Golgi-associated PDZ and coiled-coil motif-containing protein), represents a PDZ domain-containing protein associated with the Golgi, apparatus, which plays important roles in vesicular trafficking in, secretory and endocytic pathways. GOPC interacts with many other proteins, such as the Wnt receptors Frizzled 8 and neuroligin via its PDZ domain., Neuroligin is a neural cell-adhesion molecule of the post-synapse, which, binds to the presynapse molecule neurexin to form a heterotypic, intercellular junction. Here we report the solution structure of the GOPC, PDZ domain by NMR. Our results show that it is a canonical class I PDZ, domain, which contains two alpha-helices and six beta-strands. Using, chemical shift perturbation experiments, we further studied the binding, properties of the GOPC PDZ domain with the C-terminal motif of neuroligin., The observations showed that the ensemble of the interaction belongs to, fast exchange with low affinity. The 3D model of the GOPC PDZ, domain/neuroligin C-terminal peptide complex was constructed with the aid, of the molecular dynamics simulation method. Our discoveries provide, insight into the specific interaction of the GOPC PDZ domain with the, C-terminal peptide of Nlg and also provide a general insight about the, possible binding mode of the interaction of Nlg with other PDZ, domain-containing proteins.
Disease
Known diseases associated with this structure: Globozoospermia, 102530 (1) OMIM:[606845]
About this Structure
2DC2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of GOPC PDZ domain and its interaction with the C-terminal motif of neuroligin., Li X, Zhang J, Cao Z, Wu J, Shi Y, Protein Sci. 2006 Sep;15(9):2149-58. Epub 2006 Aug 1. PMID:16882988
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