ABCC4 p.Tyr477Trp
| Predicted by SNAP2: | A: D (75%), C: D (71%), D: D (91%), E: D (91%), F: D (53%), G: D (85%), H: D (75%), I: D (66%), K: D (91%), L: D (53%), M: D (75%), N: D (85%), P: D (95%), Q: D (85%), R: D (91%), S: D (85%), T: D (85%), V: D (71%), W: D (80%), |
| 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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[hide] The A-loop, a novel conserved aromatic acid subdom... FEBS Lett. 2006 Feb 13;580(4):1049-55. Epub 2005 Dec 22. Ambudkar SV, Kim IW, Xia D, Sauna ZE
The A-loop, a novel conserved aromatic acid subdomain upstream of the Walker A motif in ABC transporters, is critical for ATP binding.
FEBS Lett. 2006 Feb 13;580(4):1049-55. Epub 2005 Dec 22., [PMID:16412422]
Abstract [show]
ATP-binding cassette (ABC) transporters represent one of the largest families of proteins, and transport a variety of substrates ranging from ions to amphipathic anticancer drugs. The functional unit of an ABC transporter is comprised of two transmembrane domains and two cytoplasmic ABC ATPase domains. The energy of the binding and hydrolysis of ATP is used to transport the substrates across membranes. An ABC domain consists of conserved regions, the Walker A and B motifs, the signature (or C) region and the D, H and Q loops. We recently described the A-loop (Aromatic residue interacting with the Adenine ring of ATP), a highly conserved aromatic residue approximately 25 amino acids upstream of the Walker A motif that is essential for ATP-binding. Here, we review the mutational analysis of this subdomain in human P-glycoprotein as well as homology modeling, structural and data mining studies that provide evidence for a functional role of the A-loop in ATP-binding in most members of the superfamily of ABC transporters.
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No. Sentence Comment
77 For example, the substitution of Y401 with W resulted in an increase in the Km (ATP) during ATP hydrolysis and an increase in the Kd (TNPATP) in a binding assay using the fluorescent analog of ATP, TNPATP.1 Similar results were also reported for the Y477W mutant of bacterial HlyB-NBD [29].
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ABCC4 p.Tyr477Trp 16412422:77:250
status: NEW