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Protein farnesyltransferase

H W Park¹, L S Beese

¹Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.

Current Opinion in Structural Biology

|January 22, 1998

Summary

Researchers determined the crystal structure of rat protein farnesyltransferase. This enzyme is crucial for cell signaling and may help develop new cancer drugs.

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Area of Science:

Biochemistry
Structural Biology
Molecular Biology

Background:

Protein farnesyltransferase is essential for post-translational lipidation of proteins like Ras.
This lipidation is critical for cellular signal transduction pathways.
Understanding farnesyltransferase is key to comprehending protein prenylation.

Purpose of the Study:

To determine the high-resolution crystal structure of rat alpha beta heterodimeric protein farnesyltransferase.
To provide a structural basis for understanding the enzyme's mechanism and specificity.
To explore the potential for designing novel anticancer therapeutics based on the enzyme's structure.

Main Methods:

X-ray crystallography was used to determine the protein structure.
The reported resolution was 2.25 Angstroms.
Analysis of the crystal structure provided insights into enzyme-protein interactions.

Main Results:

The crystal structure of rat protein farnesyltransferase was elucidated at 2.25 A resolution.
The structure reveals details of the enzyme's active site and substrate-binding pocket.
This structural information lays the groundwork for mechanistic studies.

Conclusions:

The determined crystal structure of protein farnesyltransferase offers a detailed molecular view of this essential enzyme.
This structural insight is vital for understanding protein prenylation and its role in cell signaling.
The findings may facilitate the rational design of targeted anticancer drugs.

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