ABCMdb

ABCC7 p.Tyr563Cys

ClinVar:	c.1687T>A , p.Tyr563Asn D , Pathogenic c.1687T>G , p.Tyr563Asp ? , not provided
CF databases:	c.1687T>C , p.Tyr563His (CFTR1) D , c.1687T>A , p.Tyr563Asn (CFTR1) ? , This mutation is found in a single family with 2 PS patients, but the mutation in the other chromosome is unknown. c.1687T>G , p.Tyr563Asp (CFTR1) ? , The Y563D mutation was detected on one African-American CF chromosome of 50 screened. It was not detected on any of 208 normal African-American chromosomes by ASO analysis. The patient is a 9 year old pancreatic insufficient male with mild lung disease. c.1688A>G , p.Tyr563Cys (CFTR1) ? , The above mutation was detected by SSCP and identified by direct sequencing. The mutation destroys an AccI site which was used for confirmation.
Predicted by SNAP2:	A: D (95%), C: D (95%), D: D (95%), E: D (95%), F: D (95%), G: D (95%), H: D (95%), I: D (95%), K: D (95%), L: D (91%), M: D (95%), N: D (75%), P: D (95%), Q: D (95%), R: D (95%), S: D (95%), T: D (95%), V: D (95%), W: D (95%),
Predicted by PROVEAN:	A: D, C: D, D: D, E: D, F: D, G: D, H: D, I: D, K: D, L: D, M: D, N: D, P: D, Q: D, R: D, S: D, T: D, V: D, W: D,

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Publications
[hide] Nucleotide binding domains of human CFTR: a struct... Cell Mol Life Sci. 2005 Sep;62(18):2112-23. Eudes R, Lehn P, Ferec C, Mornon JP, Callebaut I
Nucleotide binding domains of human CFTR: a structural classification of critical residues and disease-causing mutations.
Cell Mol Life Sci. 2005 Sep;62(18):2112-23., [PMID:16132229]

Abstract [show]
Defective function of the cystic fibrosis (CF) transmembrane conductance regulator (CFTR) causes CF, the most frequent lethal inherited disease among the Caucasian population. The structure of this chloride ion channel includes two nucleotide-binding domains (NBDs), whose ATPase activity controls channel gating. Recently, the experimental structures of mouse and human CFTR NBD1 and our model of the human CFTR NBD1/NBD2 heterodimer have provided new insights into specific structural features of the CFTR NBD dimer. In the present work, we provide a structural classification of CF-causing mutations which may complement the existing functional classification. Our analysis also identified amino acid residues which may play a critical role in interdomain interaction and are located at the NBD1-NBD2 interface or on the surface of the dimer. In particular, a cluster of aromatic amino acids, which includes F508 and straddles the two NBDs, might be directly involved in the interaction of the NBD1/NBD2 heterodimer with the channel-forming membrane-spanning domains.

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Sentences [show]
No. Sentence Comment
227 Missense mutations affecting Y563 (Y563N, Y563D, Y563C) have been reported, reduced levels of mature CFTR being observed for Y563N [40]. Login to comment