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Recognition of Unique Carboxyl-Terminal Motifs by Distinct PDZ Domains

Science (American Association for the Advancement of Science), 1997-01, Vol.275 (5296), p.73-77 [Peer Reviewed Journal]

Copyright 1997 American Association for the Advancement of Science ;1997 INIST-CNRS ;COPYRIGHT 1997 American Association for the Advancement of Science ;Copyright American Association for the Advancement of Science Jan 3, 1997 ;ISSN: 0036-8075 ;EISSN: 1095-9203 ;DOI: 10.1126/science.275.5296.73 ;PMID: 8974395 ;CODEN: SCIEAS

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Title:
Recognition of Unique Carboxyl-Terminal Motifs by Distinct PDZ Domains
Author: Songyang, Z. ; Fanning, A. S. ; Fu, C. ; Xu, J. ; Marfatia, S. M. ; Chishti, A. H. ; Crompton, A. ; Chan, A. C. ; Anderson, J. M. ; Cantley, L. C.
Subjects: Amino Acid Sequence ; Amino acids ; Analytical, structural and metabolic biochemistry ; Animals ; Binding and carrier proteins ; Binding Sites ; Biological and medical sciences ; Carboxylates ; Cell biology ; Cellular biology ; Coordinate systems ; Crystal structure ; Crystallography, X-Ray ; Fundamental and applied biological sciences. Psychology ; Guanine Nucleotide Exchange Factors ; Guanylate Kinases ; Helminth Proteins - chemistry ; Helminth Proteins - metabolism ; Humans ; Hydroxyls ; Kinesin - chemistry ; Kinesin - metabolism ; Libraries ; Membrane Proteins - chemistry ; Membrane Proteins - metabolism ; Mice ; Models, Molecular ; Myosins - chemistry ; Myosins - metabolism ; Nerve Tissue Proteins - chemistry ; Nerve Tissue Proteins - metabolism ; Nucleoside-Phosphate Kinase - chemistry ; Nucleoside-Phosphate Kinase - metabolism ; Peptide Library ; Peptides ; Peptides - chemistry ; Peptides - metabolism ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Tyrosine Phosphatases - chemistry ; Protein Tyrosine Phosphatases - metabolism ; Proteins ; Proteins - chemistry ; Proteins - metabolism ; Sequence Homology, Amino Acid ; T-Lymphoma Invasion and Metastasis-inducing Protein 1
Is Part Of: Science (American Association for the Advancement of Science), 1997-01, Vol.275 (5296), p.73-77
Description: The oriented peptide library technique was used to investigate the peptide-binding specificities of nine PDZ domains. Each PDZ domain selected peptides with hydrophobic residues at the carboxyl terminus. Individual PDZ domains selected unique optimal motifs defined primarily by the carboxyl terminal three to seven residues of the peptides. One family of PDZ domains, including those of the Discs Large protein, selected peptides with the consensus motif Glu-(Ser/Thr)-Xxx-(Val/Ile) (where Xxx represents any amino acid) at the carboxyl terminus. In contrast, another family of PDZ domains, including those of LIN-2, p55, and Tiam-1, selected peptides with hydrophobic or aromatic side chains at the carboxyl terminal three residues. On the basis of crystal structures of the PSD-95-3 PDZ domain, the specificities observed with the peptide library can be rationalized.
Publisher: Washington, DC: American Society for the Advancement of Science
Language: English
Identifier: ISSN: 0036-8075
EISSN: 1095-9203
DOI: 10.1126/science.275.5296.73
PMID: 8974395
CODEN: SCIEAS
Source: MEDLINE
ProQuest Central

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Recognition of Unique Carboxyl-Terminal Motifs by Distinct PDZ Domains

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