[The key role of the residue 103 in the surface interactions of gamma-crystallins].
A comparative study of intramolecular crystal interactions of two homologous gamma-crystallins II and IIIb from calf lens has been carried out. It has been shown that the key role in formation of "dimeric" associates of the head-to-tail type for gamma-crystallin IIIb is played by Met-103 which is located in the middle of the hydrophobic surface region. The absence of such a region in the molecule of gamma-crystallin II is explained by replacement of Met-103 by Ser-103. A similar alternative with the exchange of the hydrophobic residue by the hydrophilic one is observed for different gene products of gamma-crystallins from a number of vertebrates. This suggests intermolecular interaction of gamma-crystallins in the native medium of the lens.
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003459:Crystallins; D008958:Models, Molecular; D011487:Protein Conformation
D003459:Crystallins
Kliuchevaia rol' 103-go ostatka v poverkhnostnykh vzaimodeĭstviiakh gamma-kristallinov.