Related Experiment Video
Updated: Jul 14, 2026
11:14
Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins
Published on: January 6, 2017
Bence Jones KWR protein structures determined by X-ray crystallography
Debora L Makino1, Agnes H Henschen-Edman, Steven B Larson
1Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, USA.
Summary
Structural analysis of a Bence Jones protein reveals insights into plasma-cell dyscrasia. The protein
Area of Science:
- Biochemistry
- Structural Biology
- Crystallography
Background:
- Bence Jones proteins are monoclonal immunoglobulin light chains.
- These proteins are associated with plasma-cell dyscrasias like multiple myeloma.
- Understanding their structure is crucial for disease mechanisms.
Purpose of the Study:
- To determine the high-resolution crystal structure of a specific Bence Jones protein (KWR).
- To investigate the structural basis for potential amyloid fibril formation.
- To identify bound ligands within the protein structure.
Main Methods:
- X-ray diffraction analysis of crystallized Bence Jones protein (KWR).
- Structure determination in four different crystal forms.
- Analysis of protein domains, elbow angles, and ligand binding sites.
Main Results:
- The overall protein structure was conserved across different crystal forms.
- Phosphate/sulfate ions and a phenol-like ligand were identified in antigen-binding sites.
- Degraded forms at low pH or with proteolysis showed arrangements suggestive of amyloid fibrils.
Conclusions:
- The KWR Bence Jones protein structure provides a model for understanding light chain behavior.
- Structural features may predispose certain proteins to amyloid formation.
- The findings contribute to knowledge of plasma-cell dyscrasia pathogenesis.
Related Concept Videos
01:24Protein Organization
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
The primary structure of a protein is its amino acid sequence.
01:13Protein Organization
Overview
01:13Protein Organization
Overview
01:24Protein Organization
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
The primary structure of a protein is its amino acid sequence.
02:18X-ray Crystallography
The size of the unit cell and the arrangement of atoms in a crystal may be determined from measurements of the diffraction of X-rays by the crystal, termed X-ray crystallography.
Diffraction
Diffraction is the change in the direction of travel experienced by an electromagnetic wave when it encounters a physical barrier whose dimensions are comparable to those of the wavelength of the light. X-rays are electromagnetic radiation with wavelengths about as long as the distance between neighboring...
Diffraction
Diffraction is the change in the direction of travel experienced by an electromagnetic wave when it encounters a physical barrier whose dimensions are comparable to those of the wavelength of the light. X-rays are electromagnetic radiation with wavelengths about as long as the distance between neighboring...
01:22Protein Folding
Overview