Sandbox GGC11: Difference between revisions

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The following structure shows where <scene name='78/781195/Arginine120b/3'>Arg 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> Also, when Arg is mutated to Gly, it causes desmin- related myopathy, cardiomyopathy, and cataracts. Also, this mutation reduces chaperone protection activity and in some target proteins promoted aggregation. <ref name="alpha" />
The following structure shows where <scene name='78/781195/Arginine120b/3'>Arg 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> Also, when Arg is mutated to Gly, it causes desmin- related myopathy, cardiomyopathy, and cataracts. Also, this mutation reduces chaperone protection activity and in some target proteins promoted aggregation. <ref name="alpha" />


This highlight shows the location of the <scene name='78/781195/His_abr/1'>Histidine 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_abr/2'>Histidine amino acids</scene> involved in inter-subunit bridging of Zn2+ ions which enhances stability.<ref>PMID:22890888</ref> This is crucial as there is no protein turnover in the lens.  


This structure shows <scene name='78/781195/Lys72/1'>Lys 72</scene>. When this amino acid is acetylated, there might be an increase the chaperone activity for the protein. Chaperon activity is highly necessary because it plays a critical role in maintaining lens transparency. <ref>PMID:22120592</ref>
This structure shows <scene name='78/781195/Lys72/1'>Lys 72</scene>. When this amino acid is acetylated, there might be an increase the chaperone activity for the protein. Chaperon activity is highly necessary because it plays a critical role in maintaining lens transparency. <ref>PMID:22120592</ref>
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