ABCMdb

ABCB3 p.Cys540His

Predicted by SNAP2:	A: N (87%), D: N (57%), E: N (87%), F: N (72%), G: N (78%), H: N (97%), I: N (78%), K: N (97%), L: N (93%), M: N (82%), N: N (93%), P: N (66%), Q: N (97%), R: N (97%), S: N (93%), T: N (93%), V: N (82%), W: N (61%), Y: N (72%),
Predicted by PROVEAN:	A: N, D: N, E: N, F: N, G: N, H: N, I: N, K: N, L: N, M: N, N: N, P: N, Q: N, R: N, S: N, T: N, V: N, W: N, Y: N,

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Publications
[hide] Functional cysteine-less subunits of the transport... FEBS Lett. 2003 Jan 2;533(1-3):42-6. Heintke S, Chen M, Ritz U, Lankat-Buttgereit B, Koch J, Abele R, Seliger B, Tampe R
Functional cysteine-less subunits of the transporter associated with antigen processing (TAP1 and TAP2) by de novo gene assembly.
FEBS Lett. 2003 Jan 2;533(1-3):42-6., [PMID:12505156]

Abstract [show]
Within the adaptive immune system the transporter associated with antigen processing (TAP) plays a pivotal role in loading of peptides onto major histocompatibility (MHC) class I molecules. As a central tool to investigate the structure and function of the TAP complex, we created cysteine-less human TAP subunits by de novo gene synthesis, replacing all 19 cysteines in TAP1 and TAP2. After expression in TAP-deficient human fibroblasts, cysteine-less TAP1 and TAP2 are functional with respect to adenosine triphosphate (ATP)-dependent peptide transport and inhibition by ICP47 from herpes simplex virus. Cysteine-less TAP1 and TAP2 restore maturation and intracellular trafficking of MHC class I molecules to the cell surface.

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Sentences [show]
No. Sentence Comment
85 Based on sequence alignments among TAP homologs from other species, two cysteines in TAP2 were replaced by histidine and valine (C394V and C540H). Login to comment
83 Based on sequence alignments among TAP homologs from other species, two cysteines in TAP2 were replaced by histidine and valine (C394V and C540H). Login to comment