1R10: Cystic Fibrosis Transmembrane Conductance Regulator (Cftr) Nucleotide- Binding Domain One (Nbd1) With Atp, I4122 Space Group

Cystic fibrosis transmembrane conductance regulator (CFTR) is an ATP-binding cassette (ABC) transporter that functions as a chloride channel. Nucleotide-binding domain 1 (NBD1), one of two ABC domains in CFTR, also contains sites for the predominant CF-causing mutation and, potentially, for regulatory phosphorylation. We have determined crystal structures for mouse NBD1 in unliganded, ADP- and ATP-bound states, with and without phosphorylation. This NBD1 differs from typical ABC domains in having added regulatory segments, a foreshortened subdomain interconnection, and an unusual nucleotide conformation. Moreover, isolated NBD1 has undetectable ATPase activity and its structure is essentially the same independent of ligand state. Phe508, which is commonly deleted in CF, is exposed at a putative NBD1-transmembrane interface. Our results are consistent with a CFTR mechanism, whereby channel gating occurs through ATP binding in an NBD1-NBD2 nucleotide sandwich that forms upon displacement of NBD1 regulatory segments.
PDB ID: 1R10Download
MMDB ID: 25757
PDB Deposition Date: 2003/9/23
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 3  Å
Source Organism:
Similar Structures:
Biological Unit for 1R10: monomeric; determined by author and by software (PQS)
Molecular Components in 1R10
Label Count Molecule
Protein (1 molecule)
Cystic Fibrosis Transmembrane Conductance Regulator(Gene symbol: Cftr)
Molecule annotation
Chemicals (5 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB