Preparing your results

Our searching services are busy right now. Your search will reload in five seconds.

X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules.

http://www.ncbi.nlm.nih.gov/pubmed/7644498

The WW domain has previously been described as a motif of 38 semiconserved residues found in seemingly unrelated proteins, such as dystrophin, Yes-associated protein (YAP), and two transcriptional regulators, Rsp-5 and FE65. The molecular function of the WW domain has been unknown until this time. Using a functional screen of a cDNA expression library, we have identified two putative ligands of the WW domain of YAP, which we named WBP-1 and WBP-2. Peptide sequence comparison between the two partial clones revealed a homologous region consisting of a proline-rich domain followed by a tyrosine residue (with the shared sequence PPPPY), which we shall call the PY motif. Binding assays and site-specific mutagenesis have shown that the PY motif binds with relatively high affinity and specificity to the WW domain of YAP, with the preliminary consensus XPPXY being critical for binding. Herein, we have implicated the WW domain with a role in mediating protein-protein interactions, as a variant of the paradigm set by Src homology 3 domains and their proline-rich ligands.

Pubmed ID: 7644498 RIS Download

Mesh terms: Adaptor Proteins, Signal Transducing | Amino Acid Sequence | Animals | Base Sequence | Binding Sites | Carrier Proteins | Cerebellum | Cloning, Molecular | Consensus Sequence | Conserved Sequence | DNA Primers | DNA, Complementary | Female | Gene Library | Glutathione Transferase | Humans | Lung | Molecular Sequence Data | Muscle, Skeletal | Oligodeoxyribonucleotides | Open Reading Frames | Ovary | Phosphoproteins | Polymerase Chain Reaction | Proline | Rats | Recombinant Fusion Proteins | Restriction Mapping | Sequence Homology, Amino Acid

Research resources used in this publication

None found

Research tools detected in this publication

None found

Data used in this publication

None found

Associated grants

  • Agency: NIGMS NIH HHS, Id: 5T32GM07739-16
  • Agency: NCI NIH HHS, Id: CA01605

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.