Sequence specific 1H, 13C and 15N resonance assignments of the C-terminal domain of human γS-crystallin View Full Text


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Article Info

DATE

2019-04

AUTHORS

Khandekar Jishan Bari, Shrikant Sharma, Kandala V. R. Chary

ABSTRACT

The high solubility and stability of crystallins present in the human eye lens maintains its transparency and refractive index with negligible protein turnover. Monomeric γ-crystallins and oligomeric β-crystallins are made up of highly homologous double Greek key domains. These domains are symmetric and possess higher stability as a result of the complex topology of individual Greek key motifs. γS-crystallin is one of the most abundant structural βγ-crystallins present in the human eye lens. In order to understand the structural stability of individual domains of human γS-crystallin in isolation vis-à-vis full length protein, we set out to structurally characterize its C-terminal domain (abbreviated hereafter as γS-CTD) by solution NMR. In this direction, we have cloned, over-expressed, isolated and purified the γS-CTD. The 2D [15N-1H] HSQC recorded with uniformly 13C/15N labeled γS-CTD showed a highly dispersed spectrum indicating the protein to adopt an ordered conformation. In this paper, we report almost complete sequence-specific 1H, 13C and 15N resonance assignments of γS-CTD using a suite of heteronuclear 3D NMR experiments. More... »

PAGES

43-47

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s12104-018-9848-x

DOI

http://dx.doi.org/10.1007/s12104-018-9848-x

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1107093895

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30232732


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45 schema:description The high solubility and stability of crystallins present in the human eye lens maintains its transparency and refractive index with negligible protein turnover. Monomeric γ-crystallins and oligomeric β-crystallins are made up of highly homologous double Greek key domains. These domains are symmetric and possess higher stability as a result of the complex topology of individual Greek key motifs. γS-crystallin is one of the most abundant structural βγ-crystallins present in the human eye lens. In order to understand the structural stability of individual domains of human γS-crystallin in isolation vis-à-vis full length protein, we set out to structurally characterize its C-terminal domain (abbreviated hereafter as γS-CTD) by solution NMR. In this direction, we have cloned, over-expressed, isolated and purified the γS-CTD. The 2D [<sup>15</sup>N-<sup>1</sup>H] HSQC recorded with uniformly <sup>13</sup>C/<sup>15</sup>N labeled γS-CTD showed a highly dispersed spectrum indicating the protein to adopt an ordered conformation. In this paper, we report almost complete sequence-specific <sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N resonance assignments of γS-CTD using a suite of heteronuclear 3D NMR experiments.
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