ABCC7 p.Tyr515His
| CF databases: |
c.1545_1546delTA
,
p.Tyr515*
D
, CF-causing
c.1543T>C , p.Tyr515His (CFTR1) ? , |
| Predicted by SNAP2: | A: N (66%), C: N (82%), D: N (57%), E: N (78%), F: N (93%), G: N (57%), H: N (82%), I: N (82%), K: N (57%), L: N (82%), M: N (78%), N: N (72%), P: D (53%), Q: N (72%), R: N (61%), S: N (66%), T: N (72%), V: N (82%), W: N (82%), |
| Predicted by PROVEAN: | A: N, C: D, D: N, E: N, F: N, G: D, H: N, I: D, K: N, L: D, M: N, N: N, P: D, Q: N, R: N, S: N, T: N, V: D, W: N, |
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[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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No. Sentence Comment
247 (B) Ribbon representation of the NBD aa1 - aa2 segment of the three experimental MalK structures and of mCFTR NBD1, with the CFTR F508 and MalK F98 being shown in atomic details involves the exposed F508 residue, only a few missense mutations affecting these exposed aromatic residues have been reported: H484R, Y515H, H620P, H620Q and Y1307C (http://www.genet.sickkids.on.ca/cftr).
X
ABCC7 p.Tyr515His 16132229:247:315
status: NEW