EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase.
ジャーナル・号・ページ	Science, Vol. 352, Issue 6293, Page 1542-1547, Year 2016
掲載日	2016年6月24日
著者	Kliment A Verba / Ray Yu-Ruei Wang / Akihiko Arakawa / Yanxin Liu / Mikako Shirouzu / Shigeyuki Yokoyama / David A Agard /
PubMed 要旨	The Hsp90 molecular chaperone and its Cdc37 cochaperone help stabilize and activate more than half of the human kinome. However, both the mechanism by which these chaperones assist their "client" ...The Hsp90 molecular chaperone and its Cdc37 cochaperone help stabilize and activate more than half of the human kinome. However, both the mechanism by which these chaperones assist their "client" kinases and the reason why some kinases are addicted to Hsp90 while closely related family members are independent are unknown. Our structural understanding of these interactions is lacking, as no full-length structures of human Hsp90, Cdc37, or either of these proteins with a kinase have been elucidated. Here we report a 3.9 angstrom cryo-electron microscopy structure of the Hsp90-Cdc37-Cdk4 kinase complex. Surprisingly, the two lobes of Cdk4 are completely separated with the β4-β5 sheet unfolded. Cdc37 mimics part of the kinase N lobe, stabilizing an open kinase conformation by wedging itself between the two lobes. Finally, Hsp90 clamps around the unfolded kinase β5 strand and interacts with exposed N- and C-lobe interfaces, protecting the kinase in a trapped unfolded state. On the basis of this structure and an extensive amount of previously collected data, we propose unifying conceptual and mechanistic models of chaperone-kinase interactions.
リンク	Science / PubMed:27339980 / PubMed Central
手法	EM (単粒子)
解像度	3.9 - 10.0 Å
構造データ	3337 5fwk EMDB-3337: Atomic cryoEM structure of Hsp90/Cdc37/Cdk4 complex PDB-5fwk: Atomic cryoEM structure of Hsp90-Cdc37-Cdk4 complex 手法: EM (単粒子) / 解像度: 3.9 Å EMDB-3338: Atomic cryoEM structure of Hsp90/Cdc37/Cdk4 complex 手法: EM (単粒子) / 解像度: 4.0 Å EMDB-3339: Atomic cryoEM structure of Hsp90/Cdc37/Cdk4 complex 手法: EM (単粒子) / 解像度: 5.6 Å 3340 5fwp EMDB-3340: Atomic cryoEM structure of Hsp90/Cdc37/Cdk4 complex PDB-5fwp: Atomic cryoEM structure of Hsp90-Cdc37-Cdk4 complex 手法: EM (単粒子) / 解像度: 7.2 Å 3341 5fwl EMDB-3341: Atomic cryoEM structure of Hsp90/Cdc37/Cdk4 complex PDB-5fwl: Atomic cryoEM structure of Hsp90-Cdc37-Cdk4 complex 手法: EM (単粒子) / 解像度: 9.0 Å 3342 5fwm EMDB-3342: Atomic cryoEM structure of Hsp90/Cdc37/Cdk4 complex PDB-5fwm: Atomic cryoEM structure of Hsp90-Cdc37-Cdk4 complex 手法: EM (単粒子) / 解像度: 8.0 Å EMDB-3343: Atomic cryoEM structure of Hsp90/Cdc37/Cdk4 complex 手法: EM (単粒子) / 解像度: 8.0 Å EMDB-3344: Atomic cryoEM structure of Hsp90/Cdc37/Cdk4 complex 手法: EM (単粒子) / 解像度: 10.0 Å
化合物	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP / ATP, エネルギー貯蔵分子YM ChemComp-MG*: Unknown entry / マグネシウムジカチオン
由来	homo sapiens (ヒト)
キーワード	SIGNALING PROTEIN / HSP90 / CDC37 / CDK4 / CHAPERONE / KINASE / UNFOLDING