ABCMdb

PMID: 16697012

Ramaen O, Leulliot N, Sizun C, Ulryck N, Pamlard O, Lallemand JY, Tilbeurgh H, Jacquet E
Structure of the human multidrug resistance protein 1 nucleotide binding domain 1 bound to Mg2+/ATP reveals a non-productive catalytic site.
J Mol Biol. 2006 Jun 16;359(4):940-9. Epub 2006 May 2., 2006-06-16 [PubMed]

Sentences

No. Mutations Sentence Comment

63 ABCC7 p.His667Arg ABCC7 p.Phe508Ala ABCC7 p.Phe429Ser Structure based sequence alignment of MRP1-NBD1 with MRP1-NBD2, h-CFTR-NBD1 (pdb code 1xmi, F508A F429S H667R mutant), BtuCD (pdb code 1l7v), TAP1 (pdb code 1jj7), MJ0796 (pdb code 1l2t, E171Q mutant), MJ1267 (pdb code 1g9x, N31C mutant), HisP (pdb code 1b0u) and HlyB-NBD (pdb code 1mt0). Login to comment 129 ABCC1 p.Asp793Glu ABCC1 p.Glu1455Asp The role of the catalytic carboxylate was examined from NBD1- Asp793 and NBD2-Glu1455 mutations: the Asp793Glu mutation in NBD1 enhances its hydrolytic capacity, whereas the Glu1455Asp mutation in NBD2 results in an increased affinity of NBD2 for ATP, but a reduced hydrolytic activity.25 Our model shows that the orientation of His1486 could be sensitive to the conformation of His827, which is constrained by a strong hydrogen bond with Asp793, itself possibly stabilized by the participation of Asp792 to the nucleotide-binding site in the Mg2C /ATP-bound state. Login to comment