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2NMB

DNUMB PTB DOMAIN COMPLEXED WITH A PHOSPHOTYROSINE PEPTIDE, NMR, ENSEMBLE OF STRUCTURES.

Summary for 2NMB
Entry DOI10.2210/pdb2nmb/pdb
NMR InformationBMRB: 4263
DescriptorPROTEIN (NUMB PROTEIN), PROTEIN (GPPY PEPTIDE) (2 entities in total)
Functional Keywordscomplex, signal transduction, phosphotyrosine binding domain (ptb), asymetr ic cell division, cell cycle-gene regulation complex, cell cycle/gene regulation
Biological sourceDrosophila melanogaster (fruit fly)
Cellular locationNucleus: P16554
Total number of polymer chains2
Total formula weight18790.30
Authors
Li, S.-C.,Zwahlen, C.,Vincent, S.J.F.,McGlade, C.J.,Pawson, T.,Forman-Kay, J.D. (deposition date: 1998-10-29, release date: 1998-11-04, Last modification date: 2024-10-16)
Primary citationLi, S.C.,Zwahlen, C.,Vincent, S.J.,McGlade, C.J.,Kay, L.E.,Pawson, T.,Forman-Kay, J.D.
Structure of a Numb PTB domain-peptide complex suggests a basis for diverse binding specificity.
Nat.Struct.Biol., 5:1075-1083, 1998
Cited by
PubMed 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.
PubMed: 9846878
DOI: 10.1038/4185
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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