Allosteric

Allosteric regulation is the regulation of an enzyme or protein by binding an effector molecule at the protein's allosteric site (that is, a site other than the protein's active site). Effector molecules can be positive (enhancing the protein's activity) or negative (reducing the protein's activity).

Overview[edit | edit source]

Allosteric regulation plays a crucial role in many biological processes, including cellular metabolism, gene transcription, and cell signaling. It allows for the fine-tuning of protein function, enabling a single protein to perform multiple roles in different cellular contexts.

Mechanism[edit | edit source]

Allosteric regulation involves the binding of an effector molecule at a site other than the protein's active site. This binding induces a conformational change in the protein, altering its activity. The effector molecule can either enhance or inhibit the protein's activity, depending on whether it is a positive or negative effector.

Types of Allosteric Regulation[edit | edit source]

There are two main types of allosteric regulation: homotropic and heterotropic. In homotropic regulation, the normal substrate of the protein also serves as its own allosteric regulator. In heterotropic regulation, a different molecule serves as the allosteric regulator.

Role in Disease[edit | edit source]

Allosteric regulation is implicated in a number of diseases, including cancer, neurodegenerative diseases, and metabolic disorders. Understanding the mechanisms of allosteric regulation can therefore provide insights into disease pathogenesis and potential therapeutic strategies.

See Also[edit | edit source]

Allosteric Resources
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