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The Ras Gene

The Ras Gene

The Ras-gene-encoded proteins are regulators of signaling pathways controlling cell proliferation, differentiation, or cell survival. The Ras-gene family in humans constitutes three primary members—the HRas, NRas, and KRas. These genes code for four functionally distinct yet closely related proteins—the HRas, NRas, KRas4A, and KRas4B. The involvement of mutant Ras genes in human cancer was first discovered in 1982 and is among the most common causes of human tumorigenesis.
Ras is a...

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Related Experiment Video

Updated: Mar 24, 2026

Single Droplet Digital Polymerase Chain Reaction for Comprehensive and Simultaneous Detection of Mutations in Hotspot Regions

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Structural dataset for the fast-exchanging KRAS G13D.

Jia Lu¹, John Hunter¹, Anuj Manandhar¹

¹University of Texas, Southwestern Medical Center, United States.

|March 10, 2016

Summary

This summary is machine-generated.

The KRAS G13D mutation in cancer exhibits unique clinical traits. Structural studies reveal high-resolution KRAS G13D models, explaining its distinct biochemical properties and interactions.

Keywords:

Cancer GTPase KRAS X-ray crystallography

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Area of Science:

Molecular Biology
Structural Biology
Oncology

Background:

Cancers with KRAS G13D mutations display distinct clinical behaviors compared to other KRAS mutations.
Understanding the underlying biochemical and biophysical properties of KRAS G13D is crucial for explaining these clinical differences.

Purpose of the Study:

To investigate the structural basis of the KRAS G13D mutation.
To correlate structural findings with biochemical properties and clinical observations.

Main Methods:

X-ray crystallography was employed to determine the structure of oncogenic KRAS mutants.
High-resolution X-ray diffraction datasets were obtained, including a 1.13 Å structure of KRAS G13D.

Main Results:

Atomic resolution, three-dimensional structural models of KRAS G13D were constructed with high confidence.
The structural data provides a basis for understanding defects in substrate binding kinetics and GTPase activities.
Interactions with the RAS effector RAF kinase can be elucidated through these structural models.

Conclusions:

The high-resolution structure of KRAS G13D provides critical insights into its distinct biochemical and biophysical properties.
This structural data supports the correlation between KRAS G13D's molecular characteristics and its unique clinical behavior in cancers.