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Ageing and vision: structure, stability and function of lens crystallins.
The structure, assembly, interactions, stability and post-translational modifications of the crystallins are reviewed, not only in isolation but also as part of a multi-component system. Expand
Crystal structure and assembly of a eukaryotic small heat shock protein
The 2.7 Å structure of wheat HSP16.9, a member of the small heat shock proteins (sHSPs), indicates how its α-crystallin domain and flanking extensions assemble into a dodecameric double disk, and provides a model by which members of the sHSP protein family bind unfolded substrates. Expand
Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones.
The diversity of the sHsp family indicates that care must be taken in generalizing biochemical properties and activities across different family members, and this chapter has a firmer structural foundation on which to design future experiments to build a biochemical mechanism of action. Expand
Crystal structures of alpha-crystallin domain dimers of alphaB-crystallin and Hsp20.
The structures provide a high-resolution view of a candidate functional state of an sHsp that could bind non-native client proteins or specific components from cytoprotective pathways, and provide a starting point for modelling higher assembly by defining the spatial locations of grooves and pockets in a basic dimeric assembly unit. Expand
High-resolution X-ray crystal structures of human gammaD crystallin (1.25 A) and the R58H mutant (1.15 A) associated with aculeiform cataract.
The results presented here are the first high-resolution X-ray structures of human gamma crystallins and conclude that the reduction in the solubility of the mutant is mainly due to the effect of the R58H mutation in the solution phase. Expand
Polydispersity of a mammalian chaperone: Mass spectrometry reveals the population of oligomers in αB-crystallin
The ability of mass spectrometry to quantify the relative populations of particular oligomeric states revealed that, contrary to the dimeric associations observed in other small heat-shock proteins, there is no evidence for any stable substructures of bovine αB-crystallin isolated from the lens. Expand
γN‐crystallin and the evolution of the βγ‐crystallin superfamily in vertebrates
Although well conserved throughout vertebrate evolution, γN in primates has apparently undergone major changes and possible loss of functional expression, and thus appear to be the ‘missing link’ between the β and γ crystallin lineages. Expand
The molecular structure and stability of the eye lens: X-ray analysis of γ-crystallin II
The three-dimensional structure of the eye lens protein, bovine γ-crystallin II, has been determined at 2.6 Å resolution. The protein has a two domain β-structure, folded into four remarkably similarExpand
Wrapping the alpha-crystallin domain fold in a chaperone assembly.
The 2.5A resolution structure of an sHsp from the parasitic flatworm Taenia saginata Tsp36, the first metazoan crystal structure, shows a new mode of dimerization involving N-terminal regions, which differs from that seen for non-metazoan sHsps, and indicates scope for flexible assembly of subunits. Expand
Crystal Structure of R120G Disease Mutant of Human αB-Crystallin Domain Dimer Shows Closure of a Groove
The X-ray structure of the excised ACD dimer of human αB R120G close to physiological pH is solved and it is speculated that the αBR120G mutation disturbs oligomer dynamics, causing the growth of large soluble oligomers that are toxic to cells by blocking essential processes. Expand