3GBZ
Structure of the CMGC CDK Kinase from Giardia lamblia
3GBZ の概要
| エントリーDOI | 10.2210/pdb3gbz/pdb |
| 分子名称 | Kinase, CMGC CDK (2 entities in total) |
| 機能のキーワード | ssgcid, kinase, cmgc cdk, atp-binding, nucleotide-binding, serine/threonine-protein kinase, transferase, structural genomics, seattle structural genomics center for infectious disease |
| 由来する生物種 | Giardia lamblia |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 37577.12 |
| 構造登録者 | Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2009-02-20, 公開日: 2009-03-24, 最終更新日: 2023-09-06) |
| 主引用文献 | Leibly, D.J.,Newling, P.A.,Abendroth, J.,Guo, W.,Kelley, A.,Stewart, L.J.,Van Voorhis, W. Structure of a cyclin-dependent kinase from Giardia lamblia. Acta Crystallogr.,Sect.F, 67:1084-1089, 2011 Cited by PubMed Abstract: Giardia lamblia is the etiologic agent of giardiasis, a water-borne infection that is prevalent throughout the world. The need for new therapeutics for the treatment of giardiasis is of paramount importance. Owing to the ubiquitous nature of kinases and their vital importance in organisms, they are potential drug targets. In this paper, the first structure of a cyclin-dependent kinase (CDK) from G. lamblia (GlCDK; UniProt A8BZ95) is presented. CDKs are cell-cycle-associated kinases that are actively being pursued as targets for anticancer drugs as well as for antiparasitic chemotherapy. Generally, a CDK forms a complex with its associated cyclin. This CDK-cyclin complex is active and acts as a serine/threonine protein kinase. Typically, CDKs are responsible for the transition to the next phase of the cell cycle. Although the structure of GlCDK with its associated cyclin was not solved, the 1.85 Å resolution structure of apo GlCDK and a 2.0 Å resolution structure of GlCDK in complex with adenosine monophosphate are presented and the structural differences from the orthologous human CDK2 and CDK3 are discussed. PubMed: 21904054DOI: 10.1107/S1744309111018070 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.85 Å) |
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