2ez5
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:2ez5.gif|left|200px]] | + | [[Image:2ez5.gif|left|200px]] |
| - | + | ||
| - | '''Solution Structure of the dNedd4 WW3* Domain- Comm LPSY Peptide Complex''' | + | {{Structure |
| + | |PDB= 2ez5 |SIZE=350|CAPTION= <scene name='initialview01'>2ez5</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Solution Structure of the dNedd4 WW3* Domain- Comm LPSY Peptide Complex''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2EZ5 is a [ | + | 2EZ5 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EZ5 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16531238 16531238] |
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| Line 20: | Line 29: | ||
[[Category: nedd4; ww domain; commissureless; py motif; binding affinity]] | [[Category: nedd4; ww domain; commissureless; py motif; binding affinity]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:46:07 2008'' |
Revision as of 14:46, 20 March 2008
| |||||||
| 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
Page seeded by OCA on Thu Mar 20 16:46:07 2008
