3bm9

Discovery of Benzisoxazoles as Potent Inhibitors of Chaperone Hsp90

spinqualitylabelsall models 3bm9, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3bm9 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BXZ Related: 3bmy Gene: HSP90AA1, HSP90A, HSPC1, HSPCA (Homo sapiens) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. 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 PubMed Heat shock protein 90 (Hsp90) is a molecular chaperone that is responsible for activating many signaling proteins and is a promising target in tumor biology. We have identified small-molecule benzisoxazole derivatives as Hsp90 inhibitors. Crystallographic studies show that these compounds bind in the ATP binding pocket interacting with the Asp93. Structure based optimization led to the identification of potent analogues, such as 13, with good biochemical profiles. Discovery of benzisoxazoles as potent inhibitors of chaperone heat shock protein 90.,Gopalsamy A, Shi M, Golas J, Vogan E, Jacob J, Johnson M, Lee F, Nilakantan R, Petersen R, Svenson K, Chopra R, Tam MS, Wen Y, Ellingboe J, Arndt K, Boschelli F J Med Chem. 2008 Feb 14;51(3):373-5. Epub 2008 Jan 16. PMID:18197612 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Heat Shock Proteins

Proteopedia Page Contributors and Editors (what is this?)

OCA