PKD (Polycystic Kidney Disease) domain was first identified in the polycystic kidney disease protein, polycystin-1 (PKD1 gene), and contains an Ig-like fold consisting of a beta-sandwich of seven strands in two sheets with a Greek key topology, although some members have additional strands.[1] Polycystin-1 is a large cell-surface glycoprotein involved in adhesive protein–protein and protein–carbohydrate interactions; however it is not clear if the PKD domain mediates any of these interactions.

PKD domain
Identifiers
SymbolPKD
PfamPF00801
InterProIPR000601
SMARTPKD
SCOP21b4r / SCOPe / SUPFAM
CDDcd00146
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1l0qB:353–424 2c26A:1363–1442 2c4xA:1363–1442 1b4rA:277–352 1wgoA:787–869

PKD domains are also found in other proteins, usually in the extracellular parts of proteins involved in interactions with other proteins. For example, domains with a PKD-type fold are found in archaeal S-layer proteins that protect the cell from extreme environments,[2] and in the human receptor SorCS2.[3]

Human proteins containing this domain

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GPNMB; PKD1; PKD1L1; PMEL; SORCS1; SORCS2; SORCS3

References

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  1. ^ Bycroft M, Bateman A, Clarke J, Hamill SJ, Sandford R, Thomas RL, Chothia C (1999). "The structure of a PKD domain from polycystin-1: implications for polycystic kidney disease". EMBO J. 18 (2): 297–305. doi:10.1093/emboj/18.2.297. PMC 1171124. PMID 9889186.
  2. ^ Joachimiak A, Springer TA, Zhang RG, Wang JH, Liu JH, Jing H, Takagi J, Lindgren S (2002). "Archaeal surface layer proteins contain beta propeller, PKD, and beta helix domains and are related to metazoan cell surface proteins". Structure. 10 (10): 1453–1464. doi:10.1016/S0969-2126(02)00840-7. PMID 12377130.
  3. ^ Hermans-Borgmeyer I, Hampe W, Schaller HC, Rezgaoui M (2001). "The genes for the human VPS10 domain-containing receptors are large and contain many small exons". Hum. Genet. 108 (6): 529–36. doi:10.1007/s004390100504. PMID 11499680. S2CID 23375354.
This article incorporates text from the public domain Pfam and InterPro: IPR000601