Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....

Treatment Resistant Cancers

Treatment Resistant Cancers

Cancer is the second leading cause of death in the United States. A cancer cell is genetically unstable and hence can mutate faster. They can also modify their microenvironment and escape immune surveillance. The difficulties in treating cancer are further compounded by the emergence of rapid resistance to anticancer drugs. The most common ways to attain resistance in cancer cells include alteration in drug transport and metabolism, modification of drug target, elevated DNA damage response, or...

Conserved Binding Sites

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Proteome-scale study of copper-associated proteins of Aegilops tauschii.

Computational biology and chemistry·2026

Same author

Proteome-Scale Mining of Metal-Associated Proteins of Monkeypox Virus.

Proteomics·2026

Same author

Enhancement of the electrochemical properties of BiVO<sub>4</sub>: the role of oxygen vacancies induced by Ag ion implantations.

Physical chemistry chemical physics : PCCP·2026

Same author

Genome-resolved analysis of traditional fermented biofertilizers as scalable solutions for soil restoration.

Frontiers in microbiology·2026

Same author

Bioinformatic study of copper-associated proteins of bread wheat.

Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine·2025

Same author

Computational Analysis of Iron-binding Proteins in the Mutational Landscape of Cancer.

Biological trace element research·2025

Search research articles

Related Experiment Video

Updated: May 9, 2025

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Bioinformatics Analysis of Cancer Related CBP Mutations on Copper Ion and Drug Binding.

Shilpa Chauhan¹, Ankit Thakur¹, Mahesh Kulharia²

¹Centre for Computational Biology and Bioinformatics, Central University of Himachal Pradesh, Kangra, 176206, India.

The Protein Journal

|April 29, 2025

Summary

This summary is machine-generated.

Point mutations in cancer-associated copper-binding proteins (CBPs) disrupt their structure and function. These alterations impact copper binding and drug interactions, potentially influencing cancer progression and treatment strategies.

Keywords:

Binding affinity Bioinformatic analysis Cancer Copper-binding proteins Mutations

More Related Videos

Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores

Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores

Published on: April 5, 2022

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Published on: September 7, 2019

Related Experiment Videos

Last Updated: May 9, 2025

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores

Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores

Published on: April 5, 2022

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Published on: September 7, 2019

Area of Science:

Biochemistry
Molecular Biology
Cancer Biology

Background:

Copper-binding proteins (CBPs) play critical roles in cancer development and progression.
Alterations in CBPs during malignancy can significantly affect cellular processes vital for tumor growth.

Purpose of the Study:

To identify copper-binding proteins (CBPs) within the cancer proteome using bioinformatics.
To investigate the impact of point mutations on the structure, function, and binding properties of CBPs.

Main Methods:

Bioinformatics approaches were employed to identify putative CBPs in the cancer proteome.
Mutation studies were conducted on specific CBPs (Beta-2-microglobulin and Tyrosine kinase protein ABL2) to analyze the effects of point mutations.

Main Results:

32 putative CBPs were identified, with 12 linked to metastatic spread.
Point mutations were found to cause significant structural and functional changes in CBPs.
Mutations frequently disrupt copper ion binding sites and alter drug-binding affinity in CBPs.

Conclusions:

Point mutations in CBPs disrupt intramolecular interactions and affect binding affinities for other molecules.
Understanding these mutation-induced changes in CBPs is crucial for cancer biology and therapeutic development.