ABCB3 p.Ala374Asp
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PMID: 22700967
[PubMed]
Corradi V et al: "The human transporter associated with antigen processing: molecular models to describe peptide binding competent states."
No.
Sentence
Comment
190
The mutation A374D in human TAP2 influences the efficiency of binding as well as the peptide transport specificity (67).
X
ABCB3 p.Ala374Asp 22700967:190:13
status: NEW211 It has been shown that A374D alters the peptide transport specificity (67).
X
ABCB3 p.Ala374Asp 22700967:211:23
status: NEW188 The mutation A374D in human TAP2 influences the efficiency of binding as well as the peptide transport specificity (67).
X
ABCB3 p.Ala374Asp 22700967:188:13
status: NEW209 It has been shown that A374D alters the peptide transport specificity (67).
X
ABCB3 p.Ala374Asp 22700967:209:23
status: NEW189 The mutation A374D in human TAP2 influences the efficiency of binding as well as the peptide transport specificity (67).
X
ABCB3 p.Ala374Asp 22700967:189:13
status: NEW210 It has been shown that A374D alters the peptide transport specificity (67).
X
ABCB3 p.Ala374Asp 22700967:210:23
status: NEW
PMID: 21540052
[PubMed]
Pinto RD et al: "Transporters associated with antigen processing (TAP) in sea bass (Dicentrarchus labrax, L.): molecular cloning and characterization of TAP1 and TAP2."
No.
Sentence
Comment
139
In human TAP2, a single amino acid substitution (A374D), changes the preference for the transported peptide (Armandola et al., 1996).
X
ABCB3 p.Ala374Asp 21540052:139:49
status: NEW
PMID: 10581370
[PubMed]
Abele R et al: "Function of the transport complex TAP in cellular immune recognition."
No.
Sentence
Comment
352
Moreover, two pairs of residues (217/218) and (374/ 380) of rat TAP and a single point mutation (A374D) of human TAP a¡ect the substrate speci'city [78,80].
X
ABCB3 p.Ala374Asp 10581370:352:97
status: NEW
PMID: 9510178
[PubMed]
Deverson EV et al: "Functional analysis by site-directed mutagenesis of the complex polymorphism in rat transporter associated with antigen processing."
No.
Sentence
Comment
300
In addition, a point mutation of human TAP2 residue 374 from alanine to aspartic acid resulted in some loss of permissiveness again, suggesting a significant role for this region (22).
X
ABCB3 p.Ala374Asp 9510178:300:52
status: NEW