Intrinsically Disordered Protein: Difference between revisions
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It was proposed that the unfolded nature of the IUPs provides them with advantages in recognition and binding. Although their large hydrodynamic dimensions slow down diffusion, their size provides a large target for initial molecular collisions, and the lack of rigid binding pockets permits multiple approach orientations for a binding partner, which may increase the probability of productive interactions <ref>PMID: 12065587</ref><ref name='Dunker2001'/>. In addition, IUPs allow molecular plasticity by adopting more than one conformation and binding diversity by binding to several proteins and thus many of the known hub proteins are IUPs. IUPs rapid turnover in the cell allow their tight regulation as many times needed in cell signaling and cell cycle. | It was proposed that the unfolded nature of the IUPs provides them with advantages in recognition and binding. Although their large hydrodynamic dimensions slow down diffusion, their size provides a large target for initial molecular collisions, and the lack of rigid binding pockets permits multiple approach orientations for a binding partner, which may increase the probability of productive interactions <ref>PMID: 12065587</ref><ref name='Dunker2001'/>. In addition, IUPs allow molecular plasticity by adopting more than one conformation and binding diversity by binding to several proteins and thus many of the known hub proteins are IUPs. IUPs rapid turnover in the cell allow their tight regulation as many times needed in cell signaling and cell cycle. | ||
== Evolution of IUPs == | |||
In p53, the folded DNA-binding domain is conserved, while the intrinsically disordered regions display a higher rate of mutations<ref>PMID: 23352836</ref>. | |||
== Many IUPs undergo disorder-order transition == | == Many IUPs undergo disorder-order transition == | ||
