2ez5

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ez5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ez5 OCA], [http://www.ebi.ac.uk/pdbsum/2ez5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ez5 RCSB]</span>
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[[Category: Rotin, D.]]
[[Category: Rotin, D.]]
[[Category: Skrynnikov, N R.]]
[[Category: Skrynnikov, N R.]]
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[[Category: nedd4; ww domain; commissureless; py motif; binding affinity]]
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[[Category: binding affinity]]
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[[Category: commissureless]]
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[[Category: nedd4]]
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[[Category: py motif]]
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[[Category: ww domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:46:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:55:39 2008''

Revision as of 23:55, 30 March 2008


PDB ID 2ez5

Drag the structure with the mouse to rotate
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Solution Structure of the dNedd4 WW3* Domain- Comm LPSY Peptide Complex


Overview

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 Structure

2EZ5 is a Protein complex structure of sequences from Drosophila melanogaster. Full crystallographic information is available from OCA.

Reference

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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