ABCMdb

ABCB3 p.Leu410Phe

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Publications

PMID: 16828748 [PubMed] Koch J et al: "The first N-terminal transmembrane helix of each subunit of the antigenic peptide transporter TAP is essential for independent tapasin binding."

No. Sentence Comment

21 However, previous studies suggest that TAP and tapasin interact through their TMs, since soluble human tapasin variants and a transmembrane domain point mutant (L410F) were defective in TAP association and consequently impaired in MHC class I surface presentation [21]. Login to comment

PMID: 12594855 [PubMed] Garbi N et al: "A major role for tapasin as a stabilizer of the TAP peptide transporter and consequences for MHC class I expression."

No. Sentence Comment

164 The interaction of tapasin with TAP appears to be mediated by the transmembrane (TM) region of tapasin, as suggested by a TM point mutant L410F of tapasin that fails to bind and stabilize TAP [4]. Login to comment

PMID: 12200052 [PubMed] Momburg F et al: "Tapasin-the keystone of the loading complex optimizing peptide binding by MHC class I molecules in the endoplasmic reticulum."

No. Sentence Comment

164 Furthermore, the ER retention of hTpn-L410F was partially deficient, indicating that ER retention of Tpn is not a sole function of the canonical dilysine retention motif. Login to comment
331 A functional defect in the association of HC/beta2m-Crt-Tpn with TAP is given in the presence of soluble Tpn, Tpn-L410F, or mTpn molecules in .220 cells as described above (Lehner et al., 1998; Tan et al., 2002). Login to comment
334 We have recently shown that B*4402 molecules expressed in the presence of soluble hTpn, hTpn-L410F, or mTpn were suboptimally loaded with peptides (Tan et al., 2002). Login to comment
165 Furthermore, the ER retention of hTpn-L410F was partially deficient, indicating that ER retention of Tpn is not a sole function of the canonical dilysine retention motif. Login to comment
332 A functional defect in the association of HC/beta2m-Crt-Tpn with TAP is given in the presence of soluble Tpn, Tpn-L410F, or mTpn molecules in .220 cells as described above (Lehner et al., 1998; Tan et al., 2002). Login to comment
335 We have recently shown that B*4402 molecules expressed in the presence of soluble hTpn, hTpn-L410F, or mTpn were suboptimally loaded with peptides (Tan et al., 2002). Login to comment

PMID: 11823531 [PubMed] Tan P et al: "Recruitment of MHC class I molecules by tapasin into the transporter associated with antigen processing-associated complex is essential for optimal peptide loading."

No. Sentence Comment

287 The novel TM point mutant L410F has essentially lost the capacity of wild-type Tpn to elevate TAP1 steady state levels. Login to comment
289 The partial suspension of ER retention of the L410F mutant may have contributed to the failing stabilization of TAP. Login to comment
290 The formation of complexes between Crt, hTpn-L410F, and HC (Fig. 5A) suggests, however, that the TM mutation did not significantly affect the interaction of Tpn with HC. Login to comment
327 In accordance with recent studies by the McCluskey group, who analyzed Kb - and B*2705-associated peptide spectra in the presence and absence of Tpn (12, 36), we noted a considerable overlap in the spectra derived from .220.B*4402 cells transfected with hTpn, mTpn, or hTpn-L410F. Login to comment
292 The partial suspension of ER retention of the L410F mutant may have contributed to the failing stabilization of TAP. Login to comment
293 The formation of complexes between Crt, hTpn-L410F, and HC (Fig. 5A) suggests, however, that the TM mutation did not significantly affect the interaction of Tpn with HC. Login to comment
330 In accordance with recent studies by the McCluskey group, who analyzed Kb - and B*2705-associated peptide spectra in the presence and absence of Tpn (12, 36), we noted a considerable overlap in the spectra derived from .220.B*4402 cells transfected with hTpn, mTpn, or hTpn-L410F. Login to comment