2KSR

NMR structures of TM domain of the n-Acetylcholine receptor b2 subunit

Summary for 2KSR

• Entry DOI: 10.2210/pdb2ksr/pdb
• NMR Information: BMRB: 16672
• Descriptor: Neuronal acetylcholine receptor subunit beta-2 (1 entity in total)
• Functional Keywords: nicotinic acetylcholine receptors, transmembrane domain, hfip, cell junction, cell membrane, disease mutation, disulfide bond, epilepsy, glycoprotein, ion transport, ionic channel, membrane, polymorphism, postsynaptic cell membrane, synapse, transmembrane, transport, membrane protein
• Biological source: Homo sapiens (human)
• Cellular location: Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein: P17787
• Total number of polymer chains: 1
• Total formula weight: 18474.03

Authors

Bondarenko, V.,Tillman, T.,Xu, Y.,Tang, P. (deposition date: 2010-01-12, release date: 2010-06-16, Last modification date: 2024-05-22)

Primary citation

Bondarenko, V.,Tillman, T.,Xu, Y.,Tang, P.
NMR structure of the transmembrane domain of the n-acetylcholine receptor beta2 subunit.
Biochim.Biophys.Acta, 1798:1608-1614, 2010

PubMed Abstract: Nicotinic acetylcholine receptors (nAChRs) are involved in fast synaptic transmission in the central and peripheral nervous system. Among the many different types of subunits in nAChRs, the beta2 subunit often combines with the alpha4 subunit to form alpha4beta2 pentameric channels, the most abundant subtype of nAChRs in the brain. Besides computational predictions, there is limited experimental data available on the structure of the beta2 subunit. Using high-resolution NMR spectroscopy, we solved the structure of the entire transmembrane domain (TM1234) of the beta2 subunit. We found that TM1234 formed a four-helix bundle in the absence of the extracellular and intracellular domains. The structure exhibited many similarities to those previously determined for the Torpedo nAChR and the bacterial ion channel GLIC. We also assessed the influence of the fourth transmembrane helix (TM4) on the rest of the domain. Although secondary structures and tertiary arrangements were similar, the addition of TM4 caused dramatic changes in TM3 dynamics and subtle changes in TM1 and TM2. Taken together, this study suggests that the structures of the transmembrane domains of these proteins are largely shaped by determinants inherent in their sequence, but their dynamics may be sensitive to modulation by tertiary and quaternary contacts.

PubMed: 20441771
DOI: 10.1016/j.bbamem.2010.04.014

Experimental method

SOLUTION NMR