Sandbox Reserved 1472: Difference between revisions
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== Relevance (Disease) == | == Relevance (Disease) == | ||
[[Image:Example.jpg]] | |||
== Structural highlights == | == Structural highlights == | ||
In the cryo-electron microscopy structure of the Hsp90-Cdc37-Cdk4 complex the β4-β5 sheet is unfolded which separates the two lobes of Cdk4, Cdc37 wedges itself between these lobes, and Hsp90 clamps around the β5 sheet of Cdk4<ref name="verba" />. While Cdk4 as the client protein of this complex is important because its proper functioning is the intended goal of the complex Hsp90 is the key factor in the process. The main structure of Hsp90 can be broken down into three domains; N-terminal domain (NTD), Middle domain (MD), and the C-terminal domain (CTD). The NTD is the site where ATP binds closing the "clamp", the MD is primarily the site of client binding, and the CTD is responsible for dimerization of the promoters that forms the biological unit homodimer<ref name="hoter" />. | In the cryo-electron microscopy structure of the Hsp90-Cdc37-Cdk4 complex the β4-β5 sheet is unfolded which separates the two lobes of Cdk4, Cdc37 wedges itself between these lobes, and Hsp90 clamps around the β5 sheet of Cdk4<ref name="verba" />. While Cdk4 as the client protein of this complex is important because its proper functioning is the intended goal of the complex Hsp90 is the key factor in the process. The main structure of Hsp90 can be broken down into three domains; N-terminal domain (NTD), Middle domain (MD), and the C-terminal domain (CTD). The NTD is the site where ATP binds closing the "clamp", the MD is primarily the site of client binding, and the CTD is responsible for dimerization of the promoters that forms the biological unit homodimer<ref name="hoter" />. | ||
