Publication Date:
1997-01-03
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉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 -- CA66263/CA/NCI NIH HHS/ -- DK34989/DK/NIDDK NIH HHS/ -- R01 GM056203/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jan 3;275(5296):73-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Signal Transduction, Beth Israel Hospital, and Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8974395" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
Binding Sites
;
Crystallography, X-Ray
;
Guanine Nucleotide Exchange Factors
;
Guanylate Kinase
;
Helminth Proteins/chemistry/metabolism
;
Humans
;
Kinesin/chemistry/metabolism
;
Membrane Proteins/chemistry/metabolism
;
Models, Molecular
;
Myosins/chemistry/metabolism
;
Nerve Tissue Proteins/chemistry/metabolism
;
Nucleoside-Phosphate Kinase/chemistry/metabolism
;
Peptide Library
;
Peptides/chemistry/*metabolism
;
Protein Structure, Secondary
;
Protein Structure, Tertiary
;
Protein Tyrosine Phosphatases/chemistry/metabolism
;
Proteins/chemistry/*metabolism
;
Sequence Homology, Amino Acid
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
