Peptide recognition by PTB and PDZ domains

Current Opinion in Structural Biology

Volumn 7, Issue 6, 1997, Pages 835-838

  Cowburn, David ^a  

^a ROCKEFELLER UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; PEPTIDE; PHOSPHOTYROSINE; TYROSINE;

CRYSTAL STRUCTURE; MOLECULAR RECOGNITION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SHORT SURVEY;

EID: 0031452276     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(97)80155-8     Document Type: Article

References (23)

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14. Li SC, Songyang Z, Vincent SJF, Zwahlen C, Wiley S, Cantley L, Kay LE, Forman-Kay J, Pawson T. High-affinity binding of the Drosophila numb phosphotyrosine binding domain to peptides containing a Gly-Pro-(p)Tyr motif. of special interest Proc Natl Acad Sci USA. 94:1997;7204-7209 This paper describes the novel peptide sequence recognized by the PTB domain from Drosophila Numb. The selectivity of the dNumb PTB domain was shown to be markedly different from those of the IRS-1 and Shc PTB domains in that in interacts preferentially with a GP(p)Y motif, rather than NPXpY, and does not absolutely require ligand phosphorylation for binding. The authors conclude that the PTB domain is a versatile protein module, capable of exhibiting varied binding specificities.
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20. Cabral JH, Petosa C, Sutcliffe MJ, Raza S, Byron O, Poy F, Marfatia SM, Chishti AH, Liddington RC. Crystal structure of a PDZ domain. of outstanding interest Nature. 382:1996;649-652 This paper reports the crystal structure of the third PDZ domain of the human homologue of the Drosophila disc large tumour-suppressor gene product, DlgA. A groove that runs over the surface of the domain, ending in a conserved hydrophobic pocket and a conserved arginine, was shown to be present. The authors suggest that this is the binding site for the C-terminal tripeptide motif that PDZ domains recognize.
21. Harrison SC. Peptide-surface association: the case of PDZ and PTB domains. of special interest Cell. 86:1996;341-343 The structures of PTB and PDZ domains are compared and contrasted, with specific regard to their use of β-strand complementation for ligand recognition.
22. Songyang Z, Fanning AS, Fu C, Xu J, Marfatia SM, Chishti AH, Crompton A, Chan AC, Anderson JM, Cantley LC. Recognition of unique carboxyl-terminal by distinct PDZ domains. of outstanding interest Science. 275:1997;73-77 The authors used the oriented peptide library technique to investigate the peptide-binding specificities of nine PDZ domains. Individual PDZ domains selected unique optimal motifs defined primarily by the C-terminal three to seven residues of the peptides. These results were used to rationalize the specificities observed and to speculate as to their functions.
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