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Gamma-crystallin S is a monomeric structural protein and a member of the beta/gamma-crystallin family, primarily expressed in the vertebrate eye lens, where it plays a key role in maintaining lens transparency and refractive properties. CRYGS is highly stable and resistant to aggregation under normal conditions, but mutations—such as the G18V mutation—can disrupt its structure, leading to protein aggregation and cataract formation. This protein, like other crystallins, does not have known enzymatic or pharmacological "target" activity (e.g., it is not a receptor, enzyme, or transporter), but is critically important as a structural lens protein and is implicated in hereditary and age-related cataracts due to its accumulation and post-translational modifications over time.
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