| Literature DB >> 9889186 |
M Bycroft1, A Bateman, J Clarke, S J Hamill, R Sandford, R L Thomas, C Chothia.
Abstract
Most cases of autosomal dominant polycystic kidney disease (ADPKD) are the result of mutations in the PKD1 gene. The PKD1 gene codes for a large cell-surface glycoprotein, polycystin-1, of unknown function, which, based on its predicted domain structure, may be involved in protein-protein and protein-carbohydrate interactions. Approximately 30% of polycystin-1 consists of 16 copies of a novel protein module called the PKD domain. Here we show that this domain has a beta-sandwich fold. Although this fold is common to a number of cell-surface modules, the PKD domain represents a distinct protein family. The tenth PKD domain of human and Fugu polycystin-1 show extensive conservation of surface residues suggesting that this region could be a ligand-binding site. This structure will allow the likely effects of missense mutations in a large part of the PKD1 gene to be determined.Entities:
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Year: 1999 PMID: 9889186 PMCID: PMC1171124 DOI: 10.1093/emboj/18.2.297
Source DB: PubMed Journal: EMBO J ISSN: 0261-4189 Impact factor: 11.598