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The crystal structure of human cyclin H
G Andersen1, A Poterszman, J M Egly
1Institut de Génétique et Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, Illkirch, France.
FEBS Letters
|November 11, 1996
Summary
The crystal structure of human cyclin H was determined, revealing a core structure similar to other cyclins. This finding provides insights into cyclin H
Area of Science:
- Structural Biology
- Molecular Biology
- Biochemistry
Background:
- Cyclins are key regulators of the cell cycle.
- Human cyclin H is a component of the CDK-activating kinase (CAK) complex.
- Understanding cyclin structure is crucial for deciphering cell cycle control.
Purpose of the Study:
- To determine the three-dimensional crystal structure of human cyclin H.
- To elucidate the structural basis of cyclin H function and its interactions.
Main Methods:
- X-ray crystallography was used to solve the crystal structure.
- The Multiple Isomorphous Replacement (MIR) method was employed for phase determination.
- Structure refinement was performed to achieve high resolution.
Main Results:
- The crystal structure of human cyclin H was solved at 2.6 A resolution.
- The core structure exhibits the canonical cyclin fold, characterized by two helical repeats.
- A novel N-terminal and C-terminal domain, comprising two long helices, interacts with the first helical repeat.
Conclusions:
- Human cyclin H shares structural homology with other cyclins, particularly cyclin A.
- The identified structural features provide a basis for understanding cyclin H's role in the CAK complex.
- The study offers insights into the structural diversity and conserved features of the cyclin family.