Background: During the last three decades, lens β- and γ-crystallins have found a huge number of kin from numerous taxonomical sources. Most of these proteins from invertebrates and microbes have been demonstrated or predicted to bind Ca2+ involving a distinct double-clamp motif, which is largely degenerated in lens homologues.
Scope of review: The various aspects of transformation of βγ-crystallins from a quintessential Ca2+-binding protein into a primarily structural molecule have been reviewed.
Major conclusions: In lens members of βγ-crystallins, the residues involved in Ca2+ binding have diverged considerably from the classical consensus with consequent reduction in their Ca2+-binding properties. This evolutionary change is congenial to their new role as robust constituents of lens. The exact functions of the residual affinity for Ca2+ are yet to be established.
General significance: This review highlights the significance of reduction in Ca2+-binding ability of the βγ-crystallins for lens physiology and why this residual affinity may be functionally important. This article is part of a Special Issue entitled Crystallin Biochemistry in Health and Disease.
Keywords: Ca(2+)-binding; Lens; Lens transparency; β- and γ-crystallins; βγ-Crystallin domain.
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