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: 25728769DOI: 10.1016/j.molcel.2015.01.026 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.445 Å) |
Structure validation
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