Structure of a cyclin-dependent kinase fromGiardia lamblia
| Autor: | Wenjin Guo, Lance Stewart, Jan Abendroth, Paul A. Newling, Wesley C. Van Voorhis, Angela Kelley, David J. Leibly |
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| Rok vydání: | 2011 |
| Předmět: |
Models
Molecular adenosine monophosphate Molecular Sequence Data Biophysics SSGCID Crystallography X-Ray medicine.disease_cause Biochemistry fluids and secretions cyclin Structural Biology Cyclin-dependent kinase parasitic diseases Genetics medicine Structural Communications Humans Giardia lamblia Amino Acid Sequence Protein kinase A Cyclin biology Kinase Cyclin-Dependent Kinase 2 Cyclin-dependent kinase 2 Cyclin-Dependent Kinase 3 Cyclin-dependent kinase 3 Cell cycle Condensed Matter Physics Cyclin-Dependent Kinases Protein Structure Tertiary Cell biology giardiasis Structural Homology Protein biology.protein Apoproteins Sequence Alignment |
| Zdroj: | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
| ISSN: | 1744-3091 |
| Popis: | Crystal structures of a cyclin-dependent kinase from G. lamblia are presented in both apo and AMP-bound forms. 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. |
| Databáze: | OpenAIRE |
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