ABCB3 p.Lys509Ala
Predicted by SNAP2: | A: D (91%), C: D (91%), D: D (95%), E: D (95%), F: D (95%), G: D (95%), H: D (91%), I: D (91%), L: D (95%), M: D (91%), N: D (95%), P: D (95%), Q: D (91%), R: D (91%), S: D (91%), T: D (91%), V: D (91%), W: D (95%), Y: D (95%), |
Predicted by PROVEAN: | A: D, C: D, D: D, E: D, F: D, G: D, H: D, I: D, L: D, M: D, N: D, P: D, Q: D, R: D, S: D, T: D, V: D, W: D, Y: D, |
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[hide] Distinct functions and cooperative interaction of ... Proc Natl Acad Sci U S A. 2001 Jun 19;98(13):7431-6. Epub 2001 May 29. Karttunen JT, Lehner PJ, Gupta SS, Hewitt EW, Cresswell P
Distinct functions and cooperative interaction of the subunits of the transporter associated with antigen processing (TAP).
Proc Natl Acad Sci U S A. 2001 Jun 19;98(13):7431-6. Epub 2001 May 29., [PMID:11381133]
Abstract [show]
The ATP-binding cassette (ABC) transporter TAP translocates peptides from the cytosol to awaiting MHC class I molecules in the endoplasmic reticulum. TAP is made up of the TAP1 and TAP2 polypeptides, which each possess a nucleotide binding domain (NBD). However, the role of ATP in peptide binding and translocation is poorly understood. We present biochemical and functional evidence that the NBDs of TAP1 and TAP2 are non-equivalent. Photolabeling experiments with 8-azido-ATP demonstrate a cooperative interaction between the two NBDs that can be stimulated by peptide. The substitution of key lysine residues in the Walker A motifs of TAP1 and TAP2 suggests that TAP1-mediated ATP hydrolysis is not essential for peptide translocation but that TAP2-mediated ATP hydrolysis is critical, not only for translocation, but for peptide binding.
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No. Sentence Comment
123 To explore the role of ATP hydrolysis in peptide translocation, we generated mutant polypeptides in which the ''Walker lysine`` was mutated to an alanine (K544A TAP1 and K509A TAP2).
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ABCB3 p.Lys509Ala 11381133:123:170
status: NEW122 To explore the role of ATP hydrolysis in peptide translocation, we generated mutant polypeptides in which the ''Walker lysine`` was mutated to an alanine (K544A TAP1 and K509A TAP2).
X
ABCB3 p.Lys509Ala 11381133:122:170
status: NEW