Intrinsically Disordered Protein: Difference between revisions
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Binding of natural ligands such as a variety of small molecules, substrates, cofactors, other proteins, nucleic acids or membranes may induce unstructured proteins to adopt stable structures bound to the partner, or even a secondary structure bound to the partner. In addition to the cases detailed below, other examples include [[1g3j]], [[1oct]]<ref name="tompa2002" />, and the [[Lac repressor]]. | Binding of natural ligands such as a variety of small molecules, substrates, cofactors, other proteins, nucleic acids or membranes may induce unstructured proteins to adopt stable structures bound to the partner, or even a secondary structure bound to the partner. In addition to the cases detailed below, other examples include [[1g3j]], [[1oct]]<ref name="tompa2002" />, and the [[Lac repressor]]. | ||
Some IUP sequences are able to bind to multiple partners that have <25% sequence identity, and in some cases even different folds<ref name="one-to-many">PMID: 23233352</ref>. | Some IUP sequences are able to bind to multiple partners that have <25% sequence identity, and in some cases even different folds<ref name="one-to-many">PMID: 23233352</ref>. For example, the C-terminal portion of p53 is known to bind to four different protein partners each with different folds<ref name="one-to-many" />; and the N-terminus of histone H3 binds to nine different protein partners with distinct folds<ref name="one-to-many" />. | ||
=== The human p27<sup>Kip1</sup> kinase inhibitory domain <ref>PMID: 8684460</ref> === | === The human p27<sup>Kip1</sup> kinase inhibitory domain <ref>PMID: 8684460</ref> === | ||
