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TitleToxicity of Eosinophil MBP Is Repressed by Intracellular Crystallization and Promoted by Extracellular Aggregation.
Journal, issue, pagesMol. Cell, Vol. 57, Page 1011-1021, Year 2015
Publish dateJul 22, 2014 (structure data deposition date)
AuthorsSoragni, A. / Yousefi, S. / Stoeckle, C. / Soriaga, A.B. / Sawaya, M.R. / Kozlowski, E. / Schmid, I. / Radonjic-Hoesli, S. / Boutet, S. / Williams, G.J. ...Soragni, A. / Yousefi, S. / Stoeckle, C. / Soriaga, A.B. / Sawaya, M.R. / Kozlowski, E. / Schmid, I. / Radonjic-Hoesli, S. / Boutet, S. / Williams, G.J. / Messerschmidt, M. / Seibert, M.M. / Cascio, D. / Zatsepin, N.A. / Burghammer, M. / Riekel, C. / Colletier, J.P. / Riek, R. / Eisenberg, D.S. / Simon, H.U.
External linksMol. Cell / PubMed:25728769
MethodsX-ray diffraction
Resolution1.445 Å
Structure data

PDB-4qxx:
Structure of the amyloid forming peptide GNLVS (residues 26-30) from the eosinophil major basic protein (EMBP)
Method: X-RAY DIFFRACTION / Resolution: 1.445 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / amyloid-like protofibril

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