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Sandbox GGC11
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(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
| - | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<scene name='78/781195/Aa_116/3'>Arg 116</scene>this is the right one | ||
This structure highlight shows where <scene name='78/781195/2klrarg_116/1'>Arg 116</scene> is located in the A chain. A mutation of this amino acid to cysteine will lead to cataracts. <ref name="alpha" /> | This structure highlight shows where <scene name='78/781195/2klrarg_116/1'>Arg 116</scene> is located in the A chain. A mutation of this amino acid to cysteine will lead to cataracts. <ref name="alpha" /> | ||
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The following structure shows where <scene name='78/781195/Arginine120b/1'>Arginine 120 on B chain</scene> is located. The mutation of this amino acid in the B chain of crystalline gene decreased interaction with wild-type CRYAA and CRYAB. However, it increases interactions with CRBB2 and CRYGC leading to cytoplasmic aggregation. <ref>PMID:12601044</ref> | The following structure shows where <scene name='78/781195/Arginine120b/1'>Arginine 120 on B chain</scene> is located. The mutation of this amino acid in the B chain of crystalline gene decreased interaction with wild-type CRYAA and CRYAB. However, it increases interactions with CRBB2 and CRYGC leading to cytoplasmic aggregation. <ref>PMID:12601044</ref> | ||
This highlight shows the location of the <scene name='78/781195/His_ab/1'>HIS amino acids </scene> involved in inter-subunit bridging of Zn ions which enhances stability.<ref>PMID:22890888</ref> This is crucial as there is no protein turnover in the lens. | This highlight shows the location of the <scene name='78/781195/His_ab/1'>HIS amino acids </scene> involved in inter-subunit bridging of Zn ions which enhances stability.<ref>PMID:22890888</ref> This is crucial as there is no protein turnover in the lens. | ||
| + | The following structure shows <scene name='78/781195/Crystallin/1'>Alpha Crystallin Structure</scene> with all the chains that make it up. | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 19:33, 12 November 2020
Alpha- Crystallin AB Chain
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References
- ↑ 1.0 1.1 1.2 Horwitz J. Alpha-crystallin. Exp Eye Res. 2003 Feb;76(2):145-53. doi: 10.1016/s0014-4835(02)00278-6. PMID:12565801 doi:http://dx.doi.org/10.1016/s0014-4835(02)00278-6
- ↑ Srinivas P, Narahari A, Petrash JM, Swamy MJ, Reddy GB. Importance of eye lens alpha-crystallin heteropolymer with 3:1 alphaA to alphaB ratio: stability, aggregation, and modifications. IUBMB Life. 2010 Sep;62(9):693-702. doi: 10.1002/iub.373. PMID:20836128 doi:http://dx.doi.org/10.1002/iub.373
- ↑ Fu L, Liang JJ. Alteration of protein-protein interactions of congenital cataract crystallin mutants. Invest Ophthalmol Vis Sci. 2003 Mar;44(3):1155-9. PMID:12601044
- ↑ Karmakar S, Das KP. Identification of histidine residues involved in Zn(2+) binding to alphaA- and alphaB-crystallin by chemical modification and MALDI TOF mass spectrometry. Protein J. 2012 Oct;31(7):623-40. doi: 10.1007/s10930-012-9439-0. PMID:22890888 doi:http://dx.doi.org/10.1007/s10930-012-9439-0
