ABCB3 p.Cys641Ser
| Predicted by SNAP2: | A: N (72%), D: D (59%), E: D (53%), F: D (75%), G: N (66%), H: D (66%), I: D (53%), K: D (59%), L: D (59%), M: D (71%), N: N (78%), P: D (66%), Q: N (53%), R: D (53%), S: N (87%), T: N (82%), V: N (61%), W: D (80%), Y: D (71%), |
| Predicted by PROVEAN: | A: N, D: D, E: D, F: D, G: D, H: D, I: D, K: D, L: D, M: D, N: N, P: D, Q: D, R: D, S: N, T: N, V: D, W: D, Y: D, |
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[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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No. Sentence Comment
84 FEBS 26839 19-12-02 S. Heintke et al./FEBS Letters 533 (2003) 42^46 43 by serines (C6S, C12S, C14S, C73S, C179S, C488S, C662S, C735S of TAP1; C70S, C213S, C353S, C363S, C571S, C641S of TAP2); however, cysteines located within predicted transmembrane helices were exchanged to alanines (C315A of TAP1; C197A, C209A of TAP2).
X
ABCB3 p.Cys641Ser 12505156:84:177
status: NEW82 by serines (C6S, C12S, C14S, C73S, C179S, C488S, C662S, C735S of TAP1; C70S, C213S, C353S, C363S, C571S, C641S of TAP2); however, cysteines located within predicted transmembrane helices were exchanged to alanines (C315A of TAP1; C197A, C209A of TAP2).
X
ABCB3 p.Cys641Ser 12505156:82:105
status: NEW