- SASDBU9: Terminally truncated human βB2-crystallin (Beta-crystallin B2) -
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Basic information
Entry
Database: SASBDB / ID: SASDBU9
Sample
Terminally truncated human βB2-crystallin
Beta-crystallin B2 (protein), Homo sapiens
Function / homology
Function and homology information
structural constituent of eye lens / response to stimulus / lens development in camera-type eye / visual perception / structural molecule activity / identical protein binding Similarity search - Function
Journal: Structure / Year: 2017 Title: Human βB2-Crystallin Forms a Face-en-Face Dimer in Solution: An Integrated NMR and SAXS Study. Authors: Zhaoyong Xi / Matthew J Whitley / Angela M Gronenborn / Abstract: 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 ...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.
Instrument name: Advanced Photon Source (APS) 12ID-B SAXS/WAXS City: Argonne, IL / 国: USA / Type of source: X-ray synchrotron / Wavelength: 0.08856 Å / Dist. spec. to detc.: 2 mm
Detector
Name: Pilatus 2M
Scan
Title: terminally truncated human βB2-crystallin / Measurement date: Mar 20, 2015 / Exposure time: 0.4 sec. / Number of frames: 30 / Unit: 1/A /
Min
Max
Q
0.0323
0.4499
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 167 /
Min
Max
Q
0.033081
0.394955
P(R) point
1
167
R
0
67
Result
Type of curve: single_conc /
Experimental
Porod
MW
38.6 kDa
38.6 kDa
Volume
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61.84 nm3
P(R)
P(R) error
Guinier
Guinier error
Forward scattering, I0
0.0513
0.0002
0.051
0.0004
Radius of gyration, Rg
2.076 nm
0.012
2.09 nm
0.019
Min
Max
D
-
6.7
Guinier point
2
29
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