Structure and function of the WW domain
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The cytoplasmic domain of LRAD3 contains two polyproline sequences, SPPSY and PPPPY.
“The cytoplasmic domain of LRAD3 also contains two polyproline sequences, SPPSY, and PPPPY, which represent consensus sequences that are recognized by WW domain containing proteins (Sudol, 1996; Pawson and Scott, 1997).”
From LRAD3, A Novel Low-Density Lipoprotein Receptor Family Member That Modulates Amyloid Precursor Protein Trafficking (2011) · cites this paper as Sudol, 1996
Section 2.2 identifies XPPXY as a preliminary WW-domain binding consensus and reports PPPPY as a sequence in two WW-domain ligands. Both SPPSY and PPPPY fit that consensus, but the paper does not establish that either sequence occurs in the cytoplasmic domain of LRAD3. (LLM, conf=0.88)
Experimental — accuracy not yet measuredMany WW domain-containing proteins are involved in regulatory or cell signaling processes.
“The list of proteins that contain WW domains is expanding, and many of these molecules appear to be involved in regulatory or cell signaling processes (Sudol, 1996; Pawson and Scott, 1997).”
From LRAD3, A Novel Low-Density Lipoprotein Receptor Family Member That Modulates Amyloid Precursor Protein Trafficking (2011) · cites this paper as Sudol, 1996
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References 140 · Cited by 296
Research works printed but not linked: 18
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- Authors
- Sudol, M.
- Affiliations
- Icahn School of Medicine at Mount Sinai (US)
- Corresponding author
- Sudol, Marius
- ORCID
- Sudol, Marius
- Venue
- Progress in Biophysics and Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1996
- Volume
- 65
- Issue
- 1-2
- Pages
- 113-132
- ISSN
- 0079-6107 (ISSN-L)
- OpenAlex
- W1979629343
- Cited by
- 296
- References
- 140
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 2 · 2023: 8 · 2022: 3 · 2021: 9 · 2020: 4 · 2019: 4 · 2018: 3 · 2017: 5 · 2016: 5 · 2015: 8 · 2014: 7 · 2013: 10 · 2012: 8
- FWCI
- 1.74
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Progress in Biophysics and Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Muscular Dystrophy Association
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Keywords
- WW domain, peptide ligand binding, protein-peptide interactions, protein structure-function relationship
- MeSH terms
- Alzheimer Disease, Amino Acid Sequence, Animals, Biophysics, Cell Transformation, Neoplastic, Extremities, Humans, Hyperaldosteronism, Hypertension, Kidney, Molecular Sequence Data, Peptides, Proteins, Retroviridae, Syndrome, Molecular Structure, Sequence Homology, Amino Acid, src Homology Domains, Biophysical Phenomena
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