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Structure paper

TitleTrichodysplasia spinulosa-Associated Polyomavirus Uses a Displaced Binding Site on VP1 to Engage Sialylated Glycolipids.
Journal, issue, pagesPlos Pathog., Vol. 11, Page e1005112-e1005112, Year 2015
Publish dateJul 26, 2014 (structure data deposition date)
AuthorsStroh, L.J. / Gee, G.V. / Blaum, B.S. / Dugan, A.S. / Feltkamp, M.C. / Atwood, W.J. / Stehle, T.
External linksPlos Pathog. / PubMed:26302170
MethodsX-ray diffraction
Resolution1.5 - 2.1 Å
Structure data

PDB-4u5z:
Trichodysplasia spinulosa-associated polyomavirus (TSPyV) VP1
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-4u60:
Trichodysplasia spinulosa-associated polyomavirus (TSPyV) VP1 in complex with GM1 oligosaccharide
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-4u61:
Trichodysplasia spinulosa-associated polyomavirus (TSPyV) VP1 in complex with 6'-sialyllactose
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-4u62:
Trichodysplasia spinulosa-associated polyomavirus (TSPyV) VP1 in complex with 3'-sialyllactose
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-SIA:
N-acetyl-alpha-neuraminic acid

Source
  • trichodysplasia spinulosa-associated polyomavirus
KeywordsVIRAL PROTEIN / viral coat protein / jelly-roll fold / glycan binding / carbohydrate binding

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