HSP90AB1

1QZ2, 1UYM, 2L6J, 3FWV, 3NMQ, 3PRY, 3UQ3, 5FWL, 5FWM, 5FWK332615516ENSG00000096384ENSMUSG00000023944P08238Q6PK50P11499NM_001271969NM_001271970NM_001271971NM_001271972NM_007355NM_008302NP_001258901.1NP_032328Heat shock protein HSP 90-beta also called HSP90beta is a protein that in humans is encoded by the HSP90AB1 gene.1byq: HSP90 N-TERMINAL DOMAIN BOUND TO ADP-MG1osf: Human Hsp90 in complex with 17-desmethoxy-17-N,N-Dimethylaminoethylamino-Geldanamycin1uym: HUMAN HSP90-BETA WITH PU3 (9-BUTYL-8(3,4,5-TRIMETHOXY-BENZYL)-9H-PURIN-6-YLAMINE)1yc1: Crystal Structures of human HSP90alpha complexed with dihydroxyphenylpyrazoles1yc3: Crystal Structure of human HSP90alpha complexed with dihydroxyphenylpyrazoles1yc4: Crystal structure of human HSP90alpha complexed with dihydroxyphenylpyrazoles1yer: HUMAN HSP90 GELDANAMYCIN-BINDING DOMAIN, ''CLOSED'' CONFORMATION1yes: HUMAN HSP90 GELDANAMYCIN-BINDING DOMAIN, ''OPEN'' CONFORMATION1yet: GELDANAMYCIN BOUND TO THE HSP90 GELDANAMYCIN-BINDING DOMAIN2bsm: NOVEL, POTENT SMALL MOLECULE INHIBITORS OF THE MOLECULAR CHAPERONE HSP90 DISCOVERED THROUGH STRUCTURE-BASED DESIGN2bt0: NOVEL, POTENT SMALL MOLECULE INHIBITORS OF THE MOLECULAR CHAPERONE HSP90 DISCOVERED THROUGH STRUCTURE-BASED DESIGN2byh: 3-(5-CHLORO-2,4-DIHYDROXYPHENYL)-PYRAZOLE-4-CARBOXAMIDES AS INHIBITORS OF THE HSP90 MOLECULAR CHAPERONE2byi: 3-(5-CHLORO-2,4-DIHYDROXYPHENYL)-PYRAZOLE-4-CARBOXAMIDES AS INHIBITORS OF THE HSP90 MOLECULAR CHAPERONE2bz5: STRUCTURE-BASED DISCOVERY OF A NEW CLASS OF HSP90 INHIBITORS Heat shock protein HSP 90-beta also called HSP90beta is a protein that in humans is encoded by the HSP90AB1 gene. HSP90AB1 is a molecular chaperone. Chaperones are proteins that bind to other proteins, thereby stabilizing them in an ATP-dependent manner. Chaperones stabilize new proteins during translation, mature proteins which are partially unstable but also proteins that have become partially denatured due to various kinds of cellular stress. In case proper folding or refolding is impossible, HSPs mediate protein degradation. They also have specialized functions, such as intracellular transport into organelles. Human HSPs are classified into 5 major groups according to the HNGC (HUGO gene nomenclature committee):