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Mechanical Protein Functions

Mechanical Protein Functions

Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force.

Antibody Structure

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
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Reaction Mechanisms

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For instance, the decomposition of ozone appears to follow a mechanism with two steps:

Structures of Solids

Structures of Solids

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Structural Isomerism

Structural Isomerism

Isomerism in Complexes
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Lipids include a diverse group of compounds that are largely nonpolar in nature. This is because they are hydrocarbons that include mostly nonpolar carbon-carbon or carbon-hydrogen bonds. Non-polar molecules are hydrophobic (“water fearing”), or insoluble in water. Lipids perform many different functions in a cell. Cells store energy for long-term use in the form of fats. Lipids also provide insulation from the environment for plants and animals. For example, they help keep aquatic...

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Related Experiment Video

Updated: Feb 2, 2026

Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features

Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features

Published on: March 16, 2022

ABCG2: does resolving its structure elucidate the mechanism?

Parth Kapoor¹, Aaron J Horsey¹, Megan H Cox¹

¹School of Life Sciences, University of Nottingham, Queens Medical Centre, Nottingham NG7 2UH, U.K.

Biochemical Society Transactions

|November 23, 2018

Summary

This summary is machine-generated.

The ATP-binding cassette transporter ABCG2 (ATP-binding cassette sub-family G member 2) is crucial for drug pharmacokinetics and chemotherapy resistance. Recent structural biology advances offer new insights into its mechanism and potential for inhibitor design.

Keywords:

ABC transport proteins electron microscopy molecular modelling multidrug resistance pharmacokinetics transmembrane proteins

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Area of Science:

Molecular Biology
Structural Biology
Pharmacology

Background:

ABCG2 (ATP-binding cassette sub-family G member 2) is a human membrane transporter with broad substrate specificity.
This multidrug transporter plays a significant role in drug pharmacokinetics and is implicated in chemotherapy resistance.
Previous reviews highlighted research progress and knowledge gaps concerning ABCG2's function and structure.

Purpose of the Study:

To provide an updated review of ABCG2 research, focusing on advancements in structural biology.
To evaluate how new data have improved the understanding of ABCG2's structure and mechanism.
To assess the potential for translating these findings into the design of ABCG2 inhibitors.

Main Methods:

Review and synthesis of recent scientific literature on ABCG2.
Analysis of data from cryo-electron microscopy studies.
Evaluation of structural and mechanistic insights gained over the past two years.

Main Results:

The field of ABCG2 research has advanced significantly, particularly in structural biology.
Cryo-electron microscopy has provided novel insights into the structure and mechanism of ABCG2.
New data enhance understanding of ABCG2's transport activity and conformational changes.

Conclusions:

Recent structural advancements have substantially improved our comprehension of ABCG2.
The enhanced understanding of ABCG2 structure and mechanism paves the way for rational inhibitor design.
Further research is needed to fully translate structural findings into effective therapeutic strategies.