1JEW

CRYO-EM STRUCTURE OF COXSACKIEVIRUS B3(M STRAIN) WITH ITS CELLULAR RECEPTOR, COXSACKIEVIRUS AND ADENOVIRUS RECEPTOR (CAR).

Summary for 1JEW

• Entry DOI: 10.2210/pdb1jew/pdb
• Related: 1COV 1F5W 1KAC
• Descriptor: COXSACKIEVIRUS AND ADENOVIRUS RECEPTOR, COXSACKIEVIRUS CAPSID, COAT PROTEIN VP1, COXSACKIEVIRUS CAPSID, COAT PROTEIN VP2, ... (5 entities in total)
• Functional Keywords: coxsackievirus b3, cvb3, car, cryo-em structure, icosahedral virus, virus-receptor complex, virus/receptor
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 5
• Total formula weight: 107193.61

Authors

Rossmann, M.G.,He, Y. (deposition date: 2001-06-19, release date: 2001-10-03, Last modification date: 2024-02-07)

Primary citation

He, Y.,Chipman, P.R.,Howitt, J.,Bator, C.M.,Whitt, M.A.,Baker, T.S.,Kuhn, R.J.,Anderson, C.W.,Freimuth, P.,Rossmann, M.G.
Interaction of coxsackievirus B3 with the full length coxsackievirus-adenovirus receptor.
Nat.Struct.Biol., 8:874-878, 2001

PubMed Abstract: Group B coxsackieviruses (CVB) utilize the coxsackievirus-adenovirus receptor (CAR) to recognize host cells. CAR is a membrane protein with two Ig-like extracellular domains (D1 and D2), a transmembrane domain and a cytoplasmic domain. The three-dimensional structure of coxsackievirus B3 (CVB3) in complex with full length human CAR and also with the D1D2 fragment of CAR were determined to approximately 22 A resolution using cryo-electron microscopy (cryo-EM). Pairs of transmembrane domains of CAR associate with each other in a detergent cloud that mimics a cellular plasma membrane. This is the first view of a virus-receptor interaction at this resolution that includes the transmembrane and cytoplasmic portion of the receptor. CAR binds with the distal end of domain D1 in the canyon of CVB3, similar to how other receptor molecules bind to entero- and rhinoviruses. The previously described interface of CAR with the adenovirus knob protein utilizes a side surface of D1.

PubMed: 11573093
DOI: 10.1038/nsb1001-874

Experimental method

ELECTRON MICROSCOPY (22 Å)