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TitleArc self-association and formation of virus-like capsids are mediated by an N-terminal helical coil motif.
Journal, issue, pagesFebs J., Vol. 288, Page 2930-2955, Year 2021
Publish dateApr 24, 2020 (structure data deposition date)
AuthorsEriksen, M.S. / Nikolaienko, O. / Hallin, E.I. / Grodem, S. / Bustad, H.J. / Flydal, M.I. / Merski, I. / Hosokawa, T. / Lascu, D. / Akerkar, S. ...Eriksen, M.S. / Nikolaienko, O. / Hallin, E.I. / Grodem, S. / Bustad, H.J. / Flydal, M.I. / Merski, I. / Hosokawa, T. / Lascu, D. / Akerkar, S. / Cuellar, J. / Chambers, J.J. / O'Connell, R. / Muruganandam, G. / Loris, R. / Touma, C. / Kanhema, T. / Hayashi, Y. / Stratton, M.M. / Valpuesta, J.M. / Kursula, P. / Martinez, A. / Bramham, C.R.
External linksFebs J. / PubMed:33175445
MethodsX-ray diffraction
Resolution0.95 Å
Structure data

PDB-6ytu:
Atomic-resolution structure of the coiled-coil dimerisation domain of human Arc
Method: X-RAY DIFFRACTION / Resolution: 0.95 Å

Chemicals

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL / precipitant*YM

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / Arc / oligomerisation / coiled coil / dimer

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