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KMID : 0620919960280020065
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Experimental & Molecular Medicine
1996 Volume.28 No. 2 p.65 ~ p.69
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The WW domain binds polyprolines and is involved in human diseases
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Sudol, Marius
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Abstract
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Our study of transforming genes led us to the identiication of a new protein module, the WW domain, that is found in a wide range of structural, regula ory and signaling proteins. The WW domain is fun tionally similar to the SH3 module, in that it binds :)olyproline containing ligands. However, its structure is distinct. Unexpectedly, the WW domai r-polyproline ligand connection was recently implicated in several human genetic disorders inci ing the Mendelian form of hypertension knows as Liddle´s syndrome, and indirectly in rr asct,lar dystrophy, Alzheimer´s disease and also in limb and kidney formation. Since both the WW doma n and the core motif of its ligand are relatively short (40 and 5 amino acid residues), one r. could suggest that human diseases that involve mutations of these sequences could be treated succe sfully, not only by gene therapy approaches, but al; o by low molecular weight compounds. The rigid molecular shapes represented by the p )Iypr dine cores of the WW domain ligands could 3rve is guides for rational drug design.
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