野生型人γS-晶体蛋白及其白内障相关变体γS-G18V的¹H、¹³C和¹⁵N归属
¹H, ¹³C, and ¹⁵N assignments of wild-type human γS-crystallin and its cataract-related variant γS-G18V.
作者信息
Brubaker William D, Martin Rachel W
机构信息
Department of Molecular Biology and Biochemistry, University of California, Irvine, CA, USA.
出版信息
Biomol NMR Assign. 2012 Apr;6(1):63-7. doi: 10.1007/s12104-011-9326-1. Epub 2011 Jul 7.
Abstract
We present the backbone and sidechain NMR assignments and a structural analysis of the 178-residue wild-type γS-crystallin and the cataract-related point mutant, γS-G18V. γS-crystallin is a structural component of the eye lens, which maintains its solubility and stability over many years. NMR assignments and continued structural investigations of γS-crystallin and aggregation-prone variants will advance understanding of cataract formation.
摘要
我们展示了178个残基的野生型γS-晶状体蛋白和与白内障相关的点突变体γS-G18V的主链和侧链核磁共振（NMR）归属以及结构分析。γS-晶状体蛋白是眼晶状体的一种结构成分，多年来维持其溶解性和稳定性。对γS-晶状体蛋白及其易于聚集的变体进行NMR归属和持续的结构研究将推动对白内障形成的理解。
相似文献
1
¹H, ¹³C, and ¹⁵N assignments of wild-type human γS-crystallin and its cataract-related variant γS-G18V.野生型人γS-晶体蛋白及其白内障相关变体γS-G18V的¹H、¹³C和¹⁵N归属
Biomol NMR Assign. 2012 Apr;6(1):63-7. doi: 10.1007/s12104-011-9326-1. Epub 2011 Jul 7.
2
Human αB-crystallin discriminates between aggregation-prone and function-preserving variants of a client protein.人αB-晶体蛋白区分聚集倾向和保持功能的客户蛋白变异体。
Biochim Biophys Acta Gen Subj. 2020 Mar;1864(3):129502. doi: 10.1016/j.bbagen.2019.129502. Epub 2019 Dec 5.
3
Sequence specific H, C and N resonance assignments of a cataract-related variant G57W of human γS-crystallin.人γS-晶状体蛋白与白内障相关变体G57W的序列特异性H、C和N共振归属
Biomol NMR Assign. 2018 Apr;12(1):51-55. doi: 10.1007/s12104-017-9779-y. Epub 2017 Sep 21.
4
Preferential and specific binding of human αB-crystallin to a cataract-related variant of γS-crystallin.人αB-晶体蛋白对γS-晶体蛋白白内障相关变异体的优先和特异性结合。
Structure. 2013 Dec 3;21(12):2221-7. doi: 10.1016/j.str.2013.09.017. Epub 2013 Oct 31.
5
Cataract-causing G18V eliminates the antagonization by ATP against the crowding-induced destabilization of human γS-crystallin.导致白内障的 G18V 消除了 ATP 对人 γS-晶体蛋白的拥挤诱导不稳定性的拮抗作用。
Biochem Biophys Res Commun. 2020 Sep 24;530(3):554-560. doi: 10.1016/j.bbrc.2020.07.070. Epub 2020 Aug 1.
6
The G18V CRYGS mutation associated with human cataracts increases gammaS-crystallin sensitivity to thermal and chemical stress.与人类白内障相关的G18V CRYGS突变增加了γS-晶状体蛋白对热应激和化学应激的敏感性。
Biochemistry. 2009 Aug 4;48(30):7334-41. doi: 10.1021/bi900467a.
7
Increased hydrophobic surface exposure in the cataract-related G18V variant of human γS-crystallin.人γS-晶体蛋白与白内障相关的G18V变体中疏水性表面暴露增加。
Biochim Biophys Acta. 2016 Jan;1860(1 Pt B):325-32. doi: 10.1016/j.bbagen.2015.09.022. Epub 2015 Oct 14.
8
Multiple Aggregation Pathways in Human γS-Crystallin and Its Aggregation-Prone G18V Variant.人γS-晶状体蛋白及其易聚集的G18V变体中的多种聚集途径。
Invest Ophthalmol Vis Sci. 2017 Apr 1;58(4):2397-2405. doi: 10.1167/iovs.16-20621.
9
Conformational dynamics study on human γS-crystallin as an efficient route to childhood blindness.人类 γS-晶体蛋白构象动力学研究：治疗儿童盲症的有效途径
Biochem Biophys Res Commun. 2019 Apr 9;511(3):679-684. doi: 10.1016/j.bbrc.2019.02.124. Epub 2019 Feb 28.
10
Separating instability from aggregation propensity in γS-crystallin variants.分离 γS-晶体蛋白变异体中的不稳定性和聚集倾向。
Biophys J. 2011 Jan 19;100(2):498-506. doi: 10.1016/j.bpj.2010.12.3691.
引用本文的文献
1
Mini-αA-crystallin protects a client lens protein from catastrophic aggregation due to heat stress.微小αA-晶体蛋白可保护晶状体蛋白免受热应激导致的灾难性聚集。
Protein Sci. 2025 Jul;34(7):e70199. doi: 10.1002/pro.70199.
2
The Eye Lens Protein, γS Crystallin, Undergoes Glutathionylation-Induced Disulfide Bonding Between Cysteines 22 and 26.眼晶状体蛋白γS晶状体蛋白在半胱氨酸22和26之间发生谷胱甘肽化诱导的二硫键形成。
Biomolecules. 2025 Mar 11;15(3):402. doi: 10.3390/biom15030402.
3
Characterization of the Interaction of Human γS Crystallin with Metal Ions and Its Effect on Protein Aggregation.人γS晶状体蛋白与金属离子的相互作用及其对蛋白质聚集的影响的表征
Biomolecules. 2024 Dec 21;14(12):1644. doi: 10.3390/biom14121644.
4
A simple vapor-diffusion method enables protein crystallization inside the HARE serial crystallography chip.一种简单的蒸气扩散法可实现在 HARE 串联结晶芯片内的蛋白质结晶。
Acta Crystallogr D Struct Biol. 2021 Jun 1;77(Pt 6):820-834. doi: 10.1107/S2059798321003855. Epub 2021 May 19.
5
Cumulative deamidations of the major lens protein γS-crystallin increase its aggregation during unfolding and oxidation.主要晶状体蛋白γS-晶体蛋白的累积脱酰胺作用会增加其在展开和氧化过程中的聚集。
Protein Sci. 2020 Sep;29(9):1945-1963. doi: 10.1002/pro.3915.
6
Human γS-Crystallin-Copper Binding Helps Buffer against Aggregation Caused by Oxidative Damage.人 γS-晶体蛋白-铜结合有助于缓冲氧化损伤引起的聚集。
Biochemistry. 2020 Jun 30;59(25):2371-2385. doi: 10.1021/acs.biochem.0c00293. Epub 2020 Jun 12.
7
Function and Aggregation in Structural Eye Lens Crystallins.结构型眼晶状体蛋白的功能与聚集
Acc Chem Res. 2020 Apr 21;53(4):863-874. doi: 10.1021/acs.accounts.0c00014. Epub 2020 Apr 9.
8
Human αB-crystallin discriminates between aggregation-prone and function-preserving variants of a client protein.人αB-晶体蛋白区分聚集倾向和保持功能的客户蛋白变异体。
Biochim Biophys Acta Gen Subj. 2020 Mar;1864(3):129502. doi: 10.1016/j.bbagen.2019.129502. Epub 2019 Dec 5.
9
Divalent Cations and the Divergence of -Crystallin Function.二价阳离子与 β-晶状体蛋白功能的分歧。
Biochemistry. 2019 Nov 12;58(45):4505-4518. doi: 10.1021/acs.biochem.9b00507. Epub 2019 Nov 1.
10
Altered Protein Dynamics and Increased Aggregation of Human γS-Crystallin Due to Cataract-Associated Deamidations.白内障相关脱酰胺导致人 γS-晶体蛋白结构动力学改变和聚集增加。
Biochemistry. 2019 Oct 8;58(40):4112-4124. doi: 10.1021/acs.biochem.9b00593. Epub 2019 Sep 26.
本文引用的文献
1
Separating instability from aggregation propensity in γS-crystallin variants.分离 γS-晶体蛋白变异体中的不稳定性和聚集倾向。
Biophys J. 2011 Jan 19;100(2):498-506. doi: 10.1016/j.bpj.2010.12.3691.
2
Characterization of a transient unfolding intermediate in a core mutant of γS-crystallin.γS 晶体蛋白核心突变体中瞬态去折叠中间体的特性。
J Mol Biol. 2011 Jan 21;405(3):840-50. doi: 10.1016/j.jmb.2010.11.005. Epub 2010 Nov 23.
3
Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers.固态 NMR 和 SAXS 研究为 αB-晶状体蛋白寡聚物的激活提供了结构基础。
Nat Struct Mol Biol. 2010 Sep;17(9):1037-42. doi: 10.1038/nsmb.1891. Epub 2010 Aug 29.
4
The G18V CRYGS mutation associated with human cataracts increases gammaS-crystallin sensitivity to thermal and chemical stress.与人类白内障相关的G18V CRYGS突变增加了γS-晶状体蛋白对热应激和化学应激的敏感性。
Biochemistry. 2009 Aug 4;48(30):7334-41. doi: 10.1021/bi900467a.
5
Amyloid fibril formation and chaperone-like activity of peptides from alphaA-crystallin.αA-晶体蛋白衍生肽的淀粉样原纤维形成及伴侣样活性
Biochemistry. 2008 Mar 4;47(9):2961-7. doi: 10.1021/bi701823g. Epub 2008 Jan 31.
6
Solution structure of (gamma)S-crystallin by molecular fragment replacement NMR.通过分子片段置换核磁共振确定γS-晶状体蛋白的溶液结构
Protein Sci. 2005 Dec;14(12):3101-14. doi: 10.1110/ps.051635205. Epub 2005 Oct 31.
7
Gamma-S crystallin gene (CRYGS) mutation causes dominant progressive cortical cataract in humans.γ-S晶状体蛋白基因（CRYGS）突变会导致人类显性进行性皮质性白内障。
J Med Genet. 2005 Sep;42(9):706-10. doi: 10.1136/jmg.2004.028274.
8
(1)H, (15)N and (13)C resonance assignment of human gammaS-crystallin, a 21 kDa eye-lens protein.人γS-晶状体蛋白（一种21 kDa的眼晶状体蛋白）的(1)H、(15)N和(13)C共振归属
J Biomol NMR. 2004 Nov;30(3):385-6. doi: 10.1007/s10858-004-3497-3.
9
Expression and regulation of alpha-, beta-, and gamma-crystallins in mammalian lens epithelial cells.α-、β-和γ-晶状体蛋白在哺乳动物晶状体上皮细胞中的表达与调控。
Invest Ophthalmol Vis Sci. 2004 Oct;45(10):3608-19. doi: 10.1167/iovs.04-0423.
10
NMRPipe: a multidimensional spectral processing system based on UNIX pipes.NMRPipe：一个基于UNIX管道的多维光谱处理系统。
J Biomol NMR. 1995 Nov;6(3):277-93. doi: 10.1007/BF00197809.
Zotero 插件