Decreasing the homodimer interaction: a common mechanism shared by the deltaG91 mutation and deamidation in betaA3-crystallin.
Xu
Jianzhen
J
College of Bioengineering, Henan University of Technology, Zhengzhou, P.R. China. xujz0451@gmail.com
Wong
Chiwai
C
Tan
Xiaorong
X
Jing
Hongjuan
H
Zhou
Guangzhou
G
Song
Wei
W
D000577:Amides / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D006367:HeLa Cells; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008156:Luciferases; D051379:Mice; D008969:Molecular Sequence Data; D050505:Mutant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D009154:Mutation / Q000235:genetics*; D011485:Protein Binding; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D038205:beta-Crystallin A Chain / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*
D000577:Amides; C489108:CRYBA1 protein, human; D050505:Mutant Proteins; D038205:beta-Crystallin A Chain; D008156:Luciferases