ABCC7 p.Leu1065Cys
[switch to full view]Comments [show]
None has been submitted yet.
PMID: 18305154
[PubMed]
Serohijos AW et al: "Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function."
No.
Sentence
Comment
71
Cross-linking of Cys pairs F508C/L1065C, F508C/F1068C, F508C/G1069C, and F508C/F1074C confirms that Phe-508 in NBD1 associates with CL4 in MSD2 (Fig. 3 and SI Fig. 7).
X
ABCC7 p.Leu1065Cys 18305154:71:33
status: NEW81 In addition to the Phe-508-containing NBD1 surface patch, residues in other regions of the domain also interact with CL4 residues as evidenced by cross-linking of Cys pairs involving amino acids closer to the Q loop (Gln-493), including W496C/T1064C and M498C/L1065C as well as nearer the Walker B motif (Asp-572) such as K564C/G1069C (Fig. 3A and SI Fig. 8).
X
ABCC7 p.Leu1065Cys 18305154:81:260
status: NEW97 Phe-508 participates in an apparent aromatic cluster with residues from CL4(seealsoSIFig.10).CL4alsointeractswithotherregionsinNBD1assuggested by cross-linking of residues close to the Q loop (W496C/T1064C and M498C/ L1065C) and a residue near the Walker B motif (K564C/G1069C).
X
ABCC7 p.Leu1065Cys 18305154:97:217
status: NEW
PMID: 18658148
[PubMed]
He L et al: "Multiple membrane-cytoplasmic domain contacts in the cystic fibrosis transmembrane conductance regulator (CFTR) mediate regulation of channel gating."
No.
Sentence
Comment
80
In agreement with what is predicted by our model, we were able to cross-link residue pairs W496C/T1064C, M498C/L1065C (19), which proves that indeed CL4 also interacts with NBD1 through the so called Q-loop (Q493).
X
ABCC7 p.Leu1065Cys 18658148:80:111
status: NEW