Sandbox k11v: Difference between revisions
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==Toxic Amyloid Small Oligomer’s atomic view== | ==Toxic Amyloid Small Oligomer’s atomic view== | ||
<StructureSection load='3l1g' size='450' side='centre' caption='Structure of alpha-beta crystallin.PDB Id:3l1g' scene=''> | <StructureSection load='3l1g' size='450' side='centre' caption='Structure of alpha-beta crystallin(ABC).PDB Id:3l1g' scene=''> | ||
The interactive Molecular Tour below assumes that you are familiar with the journal article<ref>PMID:22403391</ref>. | The interactive Molecular Tour below assumes that you are familiar with the journal article<ref>PMID:22403391</ref>. | ||
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The entire 11-residue segment KVKVLGDVIEV forms a <scene name='77/771966/K11v_in_black/2'>hairpin loop</scene> in the 3D structure of ABC.The six residue segment GDVIEV ,termed <scene name='77/771966/Gdviev_black/1'>G6V</scene>,forms fibrils and microcrystals.The microcrystals enabled us to determine the atomic structure of G6V, which proved to be a standard class 2 steric zipper, essentially an amyloid-like protofilament. | The entire 11-residue segment KVKVLGDVIEV forms a <scene name='77/771966/K11v_in_black/2'>hairpin loop</scene> in the 3D structure of ABC.The six residue segment GDVIEV ,termed <scene name='77/771966/Gdviev_black/1'>G6V</scene>,forms fibrils and microcrystals.The microcrystals enabled us to determine the atomic structure of G6V, which proved to be a standard class 2 steric zipper, essentially an amyloid-like protofilament. | ||
Amyloid fibrils and oligomer are both formed by the hairpin segment KVKVLGDVIEV.K11V forms fibrils similar to those of protein(ABC) on shaking at elevated temperature and also similar to K11V<sup>V2L</sup>(K11V-TR).The fibrils diameter range from 20 to 100 nm in electrom microscope.G6V,K11V,K11V-TR are all convertible to amyloid state,as is their parent protein ABC.Segment K11V,K11V-TR,and a sequence variant with Leu replacing Val at position 2(K11V<sup>2L</sup>) forms stable oligomers intermediate in size between monomer and fiber. | Amyloid fibrils and oligomer are both formed by the hairpin segment KVKVLGDVIEV.K11V forms fibrils similar to those of protein(ABC) on shaking at elevated temperature and also similar to K11V<sup>V2L</sup>(K11V-TR).The fibrils diameter range from 20 to 100 nm in electrom microscope.G6V,K11V,K11V-TR are all convertible to amyloid state,as is their parent protein ABC.Segment K11V,K11V-TR,and a sequence variant with Leu replacing Val at position 2(K11V<sup>2L</sup>) are capable of converting to amyloid state as their parent protein ABC and forms stable oligomers intermediate in size between monomer and fiber. | ||
ABC K11V oligomers exhibit molecular properties in common with amyloid oligomers from other disease-related proteins and oligomers were were observed to be toxic ,displaying dose-response effects similar to those of alpha-beta involved in Alzheimer's disease. | |||
K11V and K11V<sup>V2L</sup> form hexameric oligomers.K11V oligomer is of 6 chains and K11V-TR oligomer of three tandem chains.Other than the glycine linkers and the Val-to-Leu replacement, the cylindrical bodies of the six stranded K11V and the three double stranded K11V-TR oligomers are essentially identical. | K11V and K11V<sup>V2L</sup> form hexameric oligomers.K11V oligomer is of 6 chains and K11V-TR oligomer of three tandem chains.Other than the glycine linkers and the Val-to-Leu replacement, the cylindrical bodies of the six stranded K11V and the three double stranded K11V-TR oligomers are essentially identical. | ||
