例如:"lncRNA", "apoptosis", "WRKY"

The structure of a PKD domain from polycystin-1: implications for polycystic kidney disease.

EMBO J.1999 Jan 15;18(2):297-305. doi:10.1093/emboj/18.2.297
M Bycroft 1 , A Bateman , J Clarke , S J Hamill , R Sandford , R L Thomas , C Chothia
M Bycroft 1 , A Bateman , J Clarke , S J Hamill , R Sandford , R L Thomas , C Chothia
+ et al

[No authors listed]

Author information
  • 1 MRC Centre for Protein Engineering, Lensfield Road, Cambridge CB2 1EW. mb10031@cus.cam.ac.uk

摘要


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.