2ez5
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Solution Structure of the dNedd4 WW3* Domain- Comm LPSY Peptide Complex
OverviewOverview
Interactions between the WW domains of Drosophila Nedd4 (dNedd4) and, Commissureless (Comm) PY motifs promote axon crossing at the CNS midline, and muscle synaptogenesis. Here we report the solution structure of the, dNedd4 WW3* domain complexed to the second PY motif (227'TGLPSYDEALH237'), of Comm. Unexpectedly, there are interactions between WW3* and ligand, residues both N- and C-terminal to the PY motif. Residues Y232'-L236' form, a helical turn, following the PPII helical PY motif. Mutagenesis and, binding studies confirm the importance of these extensive contacts, not, simultaneously observed in other WW domain complexes, and identify a, variable loop in WW3* responsible for its high-affinity interaction. These, studies expand our general understanding of the molecular determinants, involved in WW domain-ligand recognition. In addition, they provide, insights into the specific regulation of dNedd4-mediated ubiquitination of, Comm and subsequent internalization of Comm or the Comm/Roundabout, complex, critical for CNS and muscle development.
About this StructureAbout this Structure
2EZ5 is a Protein complex structure of sequences from Drosophila melanogaster. Full crystallographic information is available from OCA.
ReferenceReference
Structural determinants for high-affinity binding in a Nedd4 WW3* domain-Comm PY motif complex., Kanelis V, Bruce MC, Skrynnikov NR, Rotin D, Forman-Kay JD, Structure. 2006 Mar;14(3):543-53. PMID:16531238
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