3ft8: Difference between revisions
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ft/3ft8_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ft/3ft8_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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[[Category: Felicetti, B]] | [[Category: Felicetti, B]] | ||
[[Category: Palan, S]] | [[Category: Palan, S]] | ||
[[Category: Alternative splicing]] | |||
[[Category: Atp-binding]] | [[Category: Atp-binding]] | ||
[[Category: Chaperone]] | [[Category: Chaperone]] | ||
[[Category: Cytoplasm]] | |||
[[Category: Hsp90 n-terminal nucleotide binding domain]] | [[Category: Hsp90 n-terminal nucleotide binding domain]] | ||
[[Category: Nucleotide-binding]] | [[Category: Nucleotide-binding]] | ||
[[Category: Phosphoprotein]] | [[Category: Phosphoprotein]] | ||
[[Category: Stress response]] | [[Category: Stress response]] | ||
Revision as of 10:26, 5 December 2018
Structure of HSP90 bound with a noval fragment.Structure of HSP90 bound with a noval fragment.
Structural highlights
Function[HS90A_HUMAN] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHeat shock protein 90 (Hsp90) plays a key role in stress response and protection of the cell against the effects of mutation. Herein we report the identification of an Hsp90 inhibitor identified by fragment screening using a high-concentration biochemical assay, as well as its optimisation by in silico searching coupled with a structure-based drug design (SBDD) approach. Fragment-based identification of Hsp90 inhibitors.,Barker JJ, Barker O, Boggio R, Chauhan V, Cheng RK, Corden V, Courtney SM, Edwards N, Falque VM, Fusar F, Gardiner M, Hamelin EM, Hesterkamp T, Ichihara O, Jones RS, Mather O, Mercurio C, Minucci S, Montalbetti CA, Muller A, Patel D, Phillips BG, Varasi M, Whittaker M, Winkler D, Yarnold CJ ChemMedChem. 2009 Jun;4(6):963-6. PMID:19301319[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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