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6UR8

CryoEM structure of human alpha4beta2 nicotinic acetylcholine receptor in complex with varenicline

Summary for 6UR8
Entry DOI10.2210/pdb6ur8/pdb
EMDB information20857
DescriptorChimera of soluble cytochrome b562 (BRIL) and neuronal acetylcholine receptor subunit alpha-4, Neuronal acetylcholine receptor subunit beta-2, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
Functional Keywordsacetylcholine receptor, nicotine, varenicline, membrane protein
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains5
Total formula weight252584.21
Authors
Alvarez, F.J.D.,Mukherjee, S.,Han, S.,Ammirati, M.,Kossiakoff, A.A. (deposition date: 2019-10-22, release date: 2020-04-29, Last modification date: 2024-11-13)
Primary citationMukherjee, S.,Erramilli, S.K.,Ammirati, M.,Alvarez, F.J.D.,Fennell, K.F.,Purdy, M.D.,Skrobek, B.M.,Radziwon, K.,Coukos, J.,Kang, Y.,Dutka, P.,Gao, X.,Qiu, X.,Yeager, M.,Eric Xu, H.,Han, S.,Kossiakoff, A.A.
Synthetic antibodies against BRIL as universal fiducial marks for single-particle cryoEM structure determination of membrane proteins.
Nat Commun, 11:1598-1598, 2020
Cited by
PubMed Abstract: We propose the concept of universal fiducials based on a set of pre-made semi-synthetic antibodies (sABs) generated by customized phage display selections against the fusion protein BRIL, an engineered variant of apocytochrome b562a. These sABs can bind to BRIL fused either into the loops or termini of different GPCRs, ion channels, receptors and transporters without disrupting their structure. A crystal structure of BRIL in complex with an affinity-matured sAB (BAG2) that bound to all systems tested delineates the footprint of interaction. Negative stain and cryoEM data of several examples of BRIL-membrane protein chimera highlight the effectiveness of the sABs as universal fiducial marks. Taken together with a cryoEM structure of sAB bound human nicotinic acetylcholine receptor, this work demonstrates that these anti-BRIL sABs can greatly enhance the particle properties leading to improved cryoEM outcomes, especially for challenging membrane proteins.
PubMed: 32221310
DOI: 10.1038/s41467-020-15363-0
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.71 Å)
Structure validation

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