ABCMdb

PMID: 20687133

Protasevich I, Yang Z, Wang C, Atwell S, Zhao X, Emtage S, Wetmore D, Hunt JF, Brouillette CG
Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1.
Protein Sci. 2010 Oct;19(10):1917-31., [PubMed]

Sentences

No. Mutations Sentence Comment

44 ABCC7 p.Arg553Gln ABCC7 p.Arg553Gln ABCC7 p.Gly550Glu ABCC7 p.Gly550Glu ABCC7 p.Arg555Lys ABCC7 p.Arg555Lys ABCC7 p.Phe429Ser ABCC7 p.Phe429Ser ABCC7 p.Phe429Ser ABCC7 p.Phe429Ser ABCC7 p.Val510Asp ABCC7 p.Val510Asp ABCC7 p.Phe494Asn ABCC7 p.Phe494Asn ABCC7 p.Phe494Asn ABCC7 p.Phe494Asn ABCC7 p.Phe494Asn ABCC7 p.Phe494Asn ABCC7 p.Gln637Arg ABCC7 p.Gln637Arg ABCC7 p.Gln637Arg ABCC7 p.Gln637Arg ABCC7 p.Gln637Arg ABCC7 p.Gln637Arg ABCC7 p.Leu636Glu hNBD1 Nameb Termini / Mutationsc Tm d DTm ¼ Tm D508 - Tm wt ( C) PDB ID 1 hNBD1-D(RI,RE) 2935c46917 387-646[D405-436] 57.7 þ 0.2 2PZE 1 (F508del)hNBD1D (RI,RE) 2935c47217 387-646[D405-436, F508del] 51.5 þ 0.3 À6.2 þ 0.3 2PZF 2 387-646[D405-436, V510D] 60.2 þ 0.4 2 387-646[D405-436, V510D, F508del] 53.0 þ 0.1 À7.2 þ 0.4 3 387-646[D405-436, F494N, Q637R] 59.2 3 387-646[D405-436, F494N, Q637R, F508del] 52.8 À6.4 4 387-646[D405-436, G550E, R553Q, R555K] 61.7 4 387-646[D405-436, G550E, R553Q, R555K,F508del] 55.7 À6.0 5 387-678[D405-436] 58.1 5 387-678[D405-436, F508del] 51.7 À6.2 6 hNBDI-315 2935c38217 389-678[F429S, F494N, Q637R] 49.8 þ 0.3 6 hNBDI-3F508del15 2935c37117 389-678[F429S, F494N, Q637R, F508del] 43.6 þ 0.1 À6.3 þ 0.3 2BBS 7 389-678[F429S, F494N, L636E5, Q637R] 50.5 þ 0.2 7 389-678[F429S, F494N, L636E, Q637R, F508del] 44.9 À6.2 þ 0.2 a DSC conducted at 1 mg/mL protein. Login to comment 61 ABCC7 p.Val510Asp ABCC7 p.Phe494Asn ABCC7 p.Gln637Arg The Teem suppressor triplet (pair 4)29 increases Tm by 4 , the V510D mutation (pair 2)30 by 2.5 , and F494N/ Q637R (pair 3) by 1.5 . Login to comment