期刊
STRUCTURE
卷 25, 期 3, 页码 496-505出版社
CELL PRESS
DOI: 10.1016/j.str.2017.02.001
关键词
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资金
- NIH [EY021193]
- Advanced Photon Source, a US Department of Energy Office of Science User Facility [DE-AC02-06CH11357]
beta gamma-Crystallins are long-lived eye lens proteins that are crucial for lens transparency and refractive power. Each beta gamma-crystallin comprises two homologous domains, which are connected by a short linker. gamma-Crystallins aremonomeric, while beta-crystallins crystallize as dimers and multimers. In the crystal, human beta B2-crystallin is a domain-swapped dimer while the N-terminally truncated beta B1-crystallin forms a faceen- face dimer. Combining and integrating data from multi-angle light scattering, nuclear magnetic resonance, and small-angle X-ray scattering of full-length and terminally truncated human beta B2-crystallin in solution, we show that both these beta B2-crystallin proteins are dimeric, possess C2 symmetry, and are more compact than domain-swapped dimers. Importantly, no inter-molecular paramagnetic relaxation enhancement effects compatible with domain swapping were detected. Our collective experimental results unambiguously demonstrate that, in solution, human beta B2-crystallin is not domain swapped and exhibits a face-en-face dimer structure similar to the crystal structure of truncated beta B1-crystallin.
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