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TitleHuman βB2-Crystallin Forms a Face-en-Face Dimer in Solution: An Integrated NMR and SAXS Study.
Journal, issue, pagesStructure, Vol. 25, Issue 3, Page 496-505, Year 2017
Publish dateMar 7, 2017
AuthorsZhaoyong Xi / Matthew J Whitley / Angela M Gronenborn /
PubMed Abstractβγ-Crystallins are long-lived eye lens proteins that are crucial for lens transparency and refractive power. Each βγ-crystallin comprises two homologous domains, which are connected by a short ...βγ-Crystallins are long-lived eye lens proteins that are crucial for lens transparency and refractive power. Each βγ-crystallin comprises two homologous domains, which are connected by a short linker. γ-Crystallins are monomeric, while β-crystallins crystallize as dimers and multimers. In the crystal, human βB2-crystallin is a domain-swapped dimer while the N-terminally truncated βB1-crystallin forms a face-en-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 βB2-crystallin in solution, we show that both these βB2-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 βB2-crystallin is not domain swapped and exhibits a face-en-face dimer structure similar to the crystal structure of truncated βB1-crystallin.
External linksStructure / PubMed:28238532 / PubMed Central
MethodsSAS (X-ray synchrotron)
Structure data

SASDBT9:
Full-length human βB2-crystallin (Beta-crystallin B2)
Method: SAXS/SANS

SASDBU9:
Terminally truncated human βB2-crystallin (Beta-crystallin B2)
Method: SAXS/SANS

Source
  • Homo sapiens (human)

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