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- Title
Structure of a Numb PTB domain-peptide complex suggests a basis for diverse binding specificity.
- Authors
Li, S C; Zwahlen, C; Vincent, S J; McGlade, C J; Kay, L E; Pawson, T; Forman-Kay, J D
- Abstract
The phosphotyrosine-binding (PTB) domain of Numb, a protein involved in asymmetric cell division, has recently been shown to bind to the adapter protein Lnx through an LDNPAY sequence, to the Numb-associated kinase (Nak) through a sequence that does not contain an NPXY motif and to GP(p)Y-containing peptides obtained from library screening. We show here that these diverse peptide sequences bind with comparable affinities to the Numb PTB domain at a common binding site on the surface of the protein. The NMR structure of the Numb PTB domain in complex with a GPpY-containing peptide reveals a novel mechanism of binding with the peptide in a helical turn that does not hydrogen bond to the PTB domain beta-sheet. These results suggest that PTB domains can potentially have multiple modes of peptide recognition and provide a structural basis from which the multiple functions of the Numb PTB domain during asymmetric cell division could arise.
- Publication
Nature structural biology, 1998, Vol 5, Issue 12, p1075
- ISSN
1072-8368
- Publication type
Journal Article
- DOI
10.1038/4185