1B4R

PKD DOMAIN 1 FROM HUMAN POLYCYSTEIN-1


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 50 
  • Conformers Submitted: 20 
  • Selection Criteria: LEAST RESTRAINT VIOLATION 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

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

Bycroft, M.Bateman, A.Clarke, J.Hamill, S.J.Sandford, R.Thomas, R.L.Chothia, C.

(1999) EMBO J 18: 297-305

  • DOI: https://doi.org/10.1093/emboj/18.2.297
  • Primary Citation of Related Structures:  
    1B4R

  • PubMed 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.


  • Organizational Affiliation

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


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (PKD1_HUMAN)80Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P98161 (Homo sapiens)
Explore P98161 
Go to UniProtKB:  P98161
PHAROS:  P98161
GTEx:  ENSG00000008710 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP98161
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 50 
  • Conformers Submitted: 20 
  • Selection Criteria: LEAST RESTRAINT VIOLATION 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

  • Released Date: 1999-01-06 
  • Deposition Author(s): Bycroft, M.

Revision History  (Full details and data files)

  • Version 1.0: 1999-01-06
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-02-16
    Changes: Database references, Derived calculations