client protein

client protein

A term of art for a protein which is manipulated or processed, as in the folding of a client protein by a chaperone.
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Also a target protein, the glucocorticoid receptor (GR) protein, will be introduced to observe how the behaviour of each domain changes upon binding a client protein.
Scientists from the US, Argentina, Israel, India, and Europe discuss electron cryptomography and its application to bacterial chemoreceptor arrays, designing symmetric protein nanomaterials, weighted ensemble simulation, eukaryotic transcription initiation machinery, biophysical models of protein evolution, rate constants and mechanisms of protein-ligand binding, the integration of bacterial small RNAs in regulatory networks, recognition of client proteins by the proteasome, chemokine receptor structures and function, progress in human Tetrahymena telomerase structure determination, the theory and modeling of RNA structure and interactions with metal ions and small molecules, and reconstructing ancient proteins to understand the causes of structure and function.
Ganetespib, an investigational drug candidate, is a selective inhibitor of heat shock protein 90 (Hsp90), a molecular chaperone which controls the folding and activation of a number of client proteins that drive tumor development and progression, added the company.
Several mTOR signaling pathway components such as mTOR, AKT and LKB1 are HSP90 client proteins.
This ATP-driven conformational cycle is regulated by specific co-chaperones, such as HSP70, Hop, immunophilins, cdc37 and p23, that complex with HSP90 and assembles into the HSP90 chaperone machinery, in order to assist the loading and release of client proteins.
These client proteins include a "who's who" list of cancer-relevant targets such as mutated p53, Bcr-Abl, Raf-1, ErbB2 and other kinases, as well as steroid hormone receptors.
Radicicol and geldanamycin frequently lead to a decrease in the activity or abundance of HSP9O's client proteins (Yen et al.
In preclinical studies, inhibiting Hsp90 causes the degradation of multiple client proteins and leads to cancer cell death.
In a commonly used ALK+ NSCLC cell line, ganetespib was shown to cause the loss of expression of the EML4-ALK fusion protein, the primary driver of this disease, as well as expression of a number of other Hsp90 client proteins implicated in tumor growth.
As a targeted inhibitor of HSP90, the product has the potential to control the proliferation of multiple solid tumors and hematological malignancies where uncontrolled tumor cell growth is dependent on the interaction between HSP90 and its client proteins, including tumor types that have become resistant to initial therapy.
In vivo, STA-9090 showed strong single-agent activity in xenograft models of human NSCLC carrying either a BRAF mutation or EML4-ALK fusion, in accordance with the sensitivity of these client proteins to the effects of STA-9090 action.
Many of the proteins which are associated with multiple myeloma are known client proteins of Hsp90 and following treatment with bortezomib, Hsp90 related proteins are known to increase as a mechanism of resistance.