Biochemical and Biophysical Research Communications
Regular ArticleWWP, a New Amino Acid Motif Present in Single or Multiple Copies in Various Proteins Including Dystrophin and the SH3-Binding Yes-Associated Protein YAP65
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Probing the ligand binding specificity of FNBP4 WW domains and interaction with FH1 domain of FMN1
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2022, Theranostics and Precision Medicine for the Management of Hepatocellular Carcinoma, Volume 2: Diagnosis, Therapeutic Targets, and Molecular MechanismsIntrinsic disorder and amino acid specificity modulate binding of the WW2 domain in kidney and brain protein (KIBRA) to synaptopodin
2019, Journal of Biological ChemistryCitation Excerpt :Two conserved tryptophans (W), from which the WW name is derived, lie on opposite sides of the β sheet. The first tryptophan is part of a hydrophobic core essential for domain stability, and the second tryptophan, located in a solvent-exposed region, is a hydrogen bond donor important in ligand binding (15). Human KIBRA WW1 and WW2 domains are separated by a 14-residue segment and recognize proline-rich motifs of the type PPXY (where P is proline, X is any amino acid, and Y is tyrosine).
Protein cross-linking tools for the construction of nanomaterials
2016, Current Opinion in BiotechnologyCitation Excerpt :So far, only a limited number of them have been exploited to direct supramolecular assembly. The so-called WW domains are small protein modules with two highly conserved tryptophans that have been identified in many signalling and regulatory proteins [75]. These modules, and their engineered variants [76] have a specific binding affinity for proline-rich peptide motifs in vitro [77–79] (Figure 3b).
The medical genetics of dystrophinopathies: Molecular genetic diagnosis and its impact on clinical practice
2013, Neuromuscular DisordersCitation Excerpt :The repeats are interrupted by two non-helical regions that together with small regions separating these homologous units from neighboring domains are known as “hinges”. Hinge 4 contains a WW domain whose function is still unknown but which is present in a variety of proteins from yeasts, nematodes and vertebrates [27]. The central hinges is thought to confer flexibility on the rod domain in response to muscle contraction [26].