ABCB3 p.Cys213Met
| Predicted by SNAP2: | A: N (66%), D: D (71%), E: D (59%), F: N (66%), G: D (53%), H: N (53%), I: N (72%), K: D (59%), L: N (82%), M: N (78%), N: N (57%), P: D (66%), Q: D (59%), R: D (59%), S: N (66%), T: N (66%), V: N (72%), W: D (59%), Y: N (61%), |
| Predicted by PROVEAN: | A: N, D: D, E: D, F: N, G: D, H: D, I: N, K: N, L: N, M: N, N: D, P: D, Q: N, R: N, S: N, T: N, V: N, W: N, Y: N, |
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[hide] The human transporter associated with antigen proc... J Biol Chem. 2012 Aug 10;287(33):28099-111. Epub 2012 Jun 14. Corradi V, Singh G, Tieleman DP
The human transporter associated with antigen processing: molecular models to describe peptide binding competent states.
J Biol Chem. 2012 Aug 10;287(33):28099-111. Epub 2012 Jun 14., [PMID:22700967]
Abstract [show]
The human transporter associated with antigen processing (TAP) is a member of the ATP binding cassette (ABC) transporter superfamily. TAP plays an essential role in the antigen presentation pathway by translocating cytosolic peptides derived from proteasomal degradation into the endoplasmic reticulum lumen. Here, the peptides are loaded into major histocompatibility class I molecules to be in turn exposed at the cell surface for recognition by T-cells. TAP is a heterodimer formed by the association of two half-transporters, TAP1 and TAP2, with a typical ABC transporter core that consists of two nucleotide binding domains and two transmembrane domains. Despite the availability of biological data, a full understanding of the mechanism of action of TAP is limited by the absence of experimental structures of the full-length transporter. Here, we present homology models of TAP built on the crystal structures of P-glycoprotein, ABCB10, and Sav1866. The models represent the transporter in inward- and outward-facing conformations that could represent initial and final states of the transport cycle, respectively. We described conserved regions in the endoplasmic reticulum-facing loops with a role in the opening and closing of the cavity. We also identified conserved pi-stacking interactions in the cytosolic part of the transmembrane domains that could explain the experimental data available for TAP1-Phe-265. Electrostatic potential calculations gave structural insights into the role of residues involved in peptide binding, such as TAP1-Val-288, TAP2-Cys-213, TAP2-Met-218. Moreover, these calculations identified additional residues potentially involved in peptide binding, in turn verified with replica exchange simulations performed on a peptide bound to the inward-facing models.
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No. Sentence Comment
265 Baldauf et al. (69) proposed that the C terminus of a bound peptide is oriented toward the Cys-213/Met-218 residues of TAP2.
X
ABCB3 p.Cys213Met 22700967:265:91
status: NEW263 Baldauf et al. (69) proposed that the C terminus of a bound peptide is oriented toward the Cys-213/Met-218 residues of TAP2.
X
ABCB3 p.Cys213Met 22700967:263:91
status: NEW264 Baldauf et al. (69) proposed that the C terminus of a bound peptide is oriented toward the Cys-213/Met-218 residues of TAP2.
X
ABCB3 p.Cys213Met 22700967:264:91
status: NEW