4QXX

Structure of the amyloid forming peptide GNLVS (residues 26-30) from the eosinophil major basic protein (EMBP)

Summary for 4QXX

Entry DOI	10.2210/pdb4qxx/pdb
Descriptor	Bone marrow proteoglycan (2 entities in total)
Functional Keywords	amyloid-like protofibril, protein fibril
Biological source	Homo sapiens (human)
Cellular location	Bone marrow proteoglycan: Secreted. Eosinophil granule major basic protein: Cytoplasmic vesicle, secretory vesicle: P13727
Total number of polymer chains	1
Total formula weight	488.54
Authors	Soriaga, A.B.,Soragni, A.,Sawaya, M.R.,Eisenberg, D. (deposition date: 2014-07-22, release date: 2015-03-18, Last modification date: 2024-02-28)
Primary citation	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. Toxicity of Eosinophil MBP Is Repressed by Intracellular Crystallization and Promoted by Extracellular Aggregation. Mol.Cell, 57:1011-1021, 2015 Cited by PubMed: 25728769 DOI: 10.1016/j.molcel.2015.01.026 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.445 Å)

Structure validation