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PMID: 8736547 Published · ppublish English Journal Article Review

WW domains.

Structure (London, England : 1993) ·Vol. 4 ·No. 5 ·1996-05-15 ·Pages 495-9

Staub O, Rotin D

Abstract

WW domains are recently described protein-protein interaction modules; they bind to proline-rich sequences that usually also contain a tyrosine. These domains have been detected in several unrelated proteins, often alongside other domains. Recent studies suggest that WW domains in specific proteins may play a role in diseases such as hypertension or muscular dystrophy.

MeSH Terms
Amino Acid Sequence Animals Consensus Sequence Dystrophin/genetics,physiology Humans Models, Chemical Molecular Sequence Data Proline/chemistry Protein Binding Proteins/chemistry Sequence Alignment Sequence Homology, Amino Acid Tyrosine/chemistry
Chemicals
Dystrophin Proteins Tyrosine Proline
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Staub O
Hospital For Sick Children, Division of Respiratory Research, Toronto, Ontario, Canada.
Rotin D
Article Info
Journal
Structure (London, England : 1993)
Abbr.
Structure
ISSN
0969-2126
Published
1996-05-15
Pages
495-9
Language
English
Region
United States
NLM ID
101087697
Subset
IM
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