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1M11

structural model of human decay-accelerating factor bound to echovirus 7 from cryo-electron microscopy

Summary for 1M11
Entry DOI10.2210/pdb1m11/pdb
Related1COV 1EV1 1G40
Descriptordecay-accelerating factor, COAT PROTEIN VP1, COAT PROTEIN VP2, ... (4 entities in total)
Functional Keywordsdecay-accelerating factor, scr, icosahedral virus, virus-receptor complex, virus/receptor
Biological sourceHomo sapiens (human)
More
Total number of polymer chains4
Total formula weight113406.87
Authors
He, Y.,Lin, F.,Chipman, P.R.,Bator, C.M.,Baker, T.S.,Shoham, M.,Kuhn, R.J.,Medof, M.E.,Rossmann, M.G. (deposition date: 2002-06-17, release date: 2002-08-28, Last modification date: 2024-02-14)
Primary citationHe, Y.,Lin, F.,Chipman, P.R.,Bator, C.M.,Baker, T.S.,Shoham, M.,Kuhn, R.J.,Medof, M.E.,Rossmann, M.G.
Structure of decay-accelerating factor bound to echovirus 7: a virus-receptor complex.
Proc.Natl.Acad.Sci.USA, 99:10325-10329, 2002
Cited by
PubMed Abstract: Echoviruses are enteroviruses that belong to Picornaviridae. Many echoviruses use decay-accelerating factor (DAF) as their cellular receptor. DAF is a glycosylphosphatidyl inositol-anchored complement regulatory protein found on most cell surfaces. It functions to protect cells from complement attack. The cryo-electron microscopy reconstructions of echovirus 7 complexed with DAF show that the DAF-binding regions are located close to the icosahedral twofold axes, in contrast to other enterovirus complexes where the viral canyon is the receptor binding site. This novel receptor binding position suggests that DAF is important for the attachment of viral particles to host cells, but probably not for initiating viral uncoating, as is the case with canyon-binding receptors. Thus, a different cell entry mechanism must be used for enteroviruses that bind DAF.
PubMed: 12119400
DOI: 10.1073/pnas.152161599
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (16 Å)
Structure validation

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