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Updated: May 18, 2026

Using X-ray Crystallography, Biophysics, and Functional Assays to Determine the Mechanisms Governing T-cell Receptor Recognition of Cancer Antigens
09:53

Using X-ray Crystallography, Biophysics, and Functional Assays to Determine the Mechanisms Governing T-cell Receptor Recognition of Cancer Antigens

Published on: February 6, 2017

Crystal structure of human multiple copies in T-cell lymphoma-1 oncoprotein

Wolfram Tempel1, Slav Dimov, Yufeng Tong

  • 1Structural Genomics Consortium, 101 College Street, MaRS South Tower, Toronto, Ontario, Canada.

Proteins
|October 9, 2012
PubMed

Insights

The oncogene multiple copies in T-cell lymphoma-1 (MCT-1) drives lymphoma. Understanding its structure reveals potential therapeutic targets for cancer treatment.

Area of Science:

  • Molecular biology
  • Structural biology
  • Oncology

Background:

  • The multiple copies in T-cell lymphoma-1 (MCT-1) oncogene is overexpressed in human lymphoma, correlating with malignant phenotypes.
  • Disrupting MCT-1 function reduces tumor formation, indicating its potential as a therapeutic target.

Purpose of the Study:

  • To elucidate the structural basis of MCT-1 function.
  • To investigate the RNA-binding capabilities of MCT-1 through structural analysis.

Main Methods:

  • Determined the crystal structure of apo MCT-1 at 1.7 Å resolution.
  • Employed the surface entropy reduction method for protein crystallization.
  • Analyzed the structural features of MCT-1, including its PUA-domain and N-terminal domain.

Main Results:

  • The C-terminus of MCT-1 exhibits a PUA-domain fold crucial for RNA recognition.
  • The N-terminal domain possesses positively charged regions predicted to mediate RNA binding.
  • The determined structure provides insights into MCT-1's molecular interactions.

Conclusions:

  • The structural data of MCT-1 supports its role as an RNA-binding protein.
  • The identified structural features offer a foundation for developing targeted MCT-1 therapies against lymphoma.

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