5l6q | pdb_00005l6q

Refolded AL protein from cardiac amyloidosis

spinqualitylabelsall models 5l6q, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5l6q is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.4Å Ligands: CL, CO3, NA, PEG, PGE, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Systemic amyloidosis is caused by the misfolding of a circulating amyloid precursor protein and the deposition of amyloid fibrils in multiple organs. Chemical and biophysical analysis of amyloid fibrils from human AL and murine AA amyloidosis reveal the same fibril morphologies in different tissues or organs of one patient or diseased animal. The observed structural similarities concerned the fibril morphology, the fibril protein primary and secondary structures, the presence of post-translational modifications and, in case of the AL fibrils, the partially folded characteristics of the polypeptide chain within the fibril. Our data imply for both analyzed forms of amyloidosis that the pathways of protein misfolding are systemically conserved; that is, they follow the same rules irrespective of where inside one body fibrils are formed or accumulated. Common Fibril Structures Imply Systemically Conserved Protein Misfolding Pathways In Vivo.,Annamalai K, Liberta F, Vielberg MT, Close W, Lilie H, Guhrs KH, Schierhorn A, Koehler R, Schmidt A, Haupt C, Hegenbart U, Schonland S, Schmidt M, Groll M, Fandrich M Angew Chem Int Ed Engl. 2017 Jun 19;56(26):7510-7514. doi:, 10.1002/anie.201701761. Epub 2017 May 23. PMID:28544119 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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