ABCC7 p.Gln637Ala
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PMID: 19927121
[PubMed]
Kanelis V et al: "NMR evidence for differential phosphorylation-dependent interactions in WT and DeltaF508 CFTR."
No.
Sentence
Comment
107
Significant conformational changes, apart from differences in the local surface properties at the mutation site, were not observed in the crystal structures of DF508 NBD1-RE (also containing F429S, F494N, and Q637A mutations required for protein solubility and crystallization) (Lewis et al, 2004, 2005) and of DF508 NBD1 lacking the RI and the RE (PDB code 2PZF).
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ABCC7 p.Gln637Ala 19927121:107:209
status: NEW249 The additional mutations (F494N, Q637A or F429S, F494N, and Q637R) in the DF508 NBD1-RE construct required for protein solubility and crystallization (Lewis et al, 2005) also partially rescue the trafficking and gating defects of full-length DF508 CFTR, suggesting that the crystal structure of DF508 NBD1-RE may correspond to a partially corrected conformation (Pissarra et al, 2008).
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ABCC7 p.Gln637Ala 19927121:249:33
status: NEW