Related Experiment Video
Updated: Jun 20, 2026
09:30
Modeling Ligands into Maps Derived from Electron Cryomicroscopy
Published on: July 19, 2024
Functional interpretation of APN receptor from M.sexta using a molecular model
Anamika Singh1, C V S Sivaprasad
1Bioinformatics and Applied Division, Indian Institute of Information Technology, Deoghat, Jhalwa, Allahabad 211012, India.
Bioinformation
|August 27, 2009
Summary
Insect resistance to Bacillus thuringiensis (Bt) toxins is a growing problem. Studying the amino-peptidase-N (APN) receptor in M. sexta insects helps understand this resistance and develop new Bt toxins for crop protection.
Area of Science:
- Agricultural Entomology
- Molecular Biology
- Biochemistry
Background:
- Synthetic pesticides cause environmental damage and insect resistance.
- Bacillus thuringiensis (Bt) is a biological alternative, but insects develop resistance to its toxins.
- Understanding insect resistance mechanisms is crucial for sustainable pest control.
Purpose of the Study:
- To investigate the molecular mechanism of insect resistance to Bt toxins.
- To analyze the amino-peptidase-N (APN) receptor in the insect M. sexta.
- To provide insights for developing novel insect-resistant Cry toxins.
Main Methods:
- Constructed a homology model of the M. sexta APN receptor using Insight II.
- Evaluated the APN model using the PROCHECK program.
- Docked oligosaccharides and analyzed predicted binding sites for ligands, metals, and Bt toxins.
Main Results:
- Developed a homology model of the M. sexta APN receptor.
- Identified potential functional sites and binding interactions of the APN receptor.
- Gained insights into receptor-toxin interactions relevant to insect resistance.
Conclusions:
- The study provides a molecular understanding of insect resistance to Bt toxins.
- The APN receptor model aids in predicting binding sites and interactions.
- This research facilitates the design of new Cry toxins for effective pest management.
Related Concept Videos
01:29The Two-State Receptor Model
The two-state receptor model explains a drug's interaction with receptors, such as G protein-coupled receptors and ligand-gated ion channels, to induce or inhibit a biological response. When no natural ligands are present, a receptor exists in an equilibrium of inactive (Ri) and active (Ra) conformations. The inactive form does not produce a response, while the active form generates a basal effect known as constitutive activity.
The binding affinity of a drug determines its interaction with one...
The binding affinity of a drug determines its interaction with one...
01:09Multi-pass Transmembrane Proteins and β-barrels
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
01:15G Protein-coupled Receptors
G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
01:30Assembly of Signaling Complexes
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
01:19Fluid Mosaic Model
Scientists identified the plasma membrane in the 1890s and its principal chemical components (lipids and proteins) by 1915. The model for plasma membrane structure, proposed in 1935 by Hugh Davson and James Danielli, was the first model to be widely accepted in the scientific community. The model was based on the plasma membrane's "railroad track" appearance in early electron micrographs. Davson and Danielli theorized that the plasma membrane's structure resembled a sandwich with the analogy of...
01:44The Significance of Membrane Transport
The transport of solutes across the cell membrane is essential for metabolic processes, like maintaining cell size and volume, generating the action potential, exchanging nutrients and gases, etc. Membrane transport can be either passive or active. It can be simple diffusion, facilitated, or mediated transport aided by transport proteins such as transporters and channels.
Transporters facilitate either an active or passive movement of solutes. They can allow a single-molecule transport down its...
Transporters facilitate either an active or passive movement of solutes. They can allow a single-molecule transport down its...