Related Experiment Video
Updated: Aug 9, 2026

11:39
Identification of Functional Protein Regions Through Chimeric Protein Construction
Published on: January 8, 2019
Homology modeling of human leptin/leptin receptor complex
1Biomolecular Engineering Research Institute, 6-2-3, Furuedai, Suita, 565-0874, Japan. toh@beri.co.jp
Biochemical and Biophysical Research Communications
|August 17, 2000
Summary
Researchers modeled the leptin receptor complex using G-CSF receptor structures. This model aids in understanding leptin
Area of Science:
- Biochemistry
- Structural Biology
- Endocrinology
Background:
- Leptin receptor is crucial for mediating leptin's weight regulatory signals.
- Understanding leptin-receptor interactions is vital for therapeutic development.
- The leptin receptor's atomic structure remains undetermined.
Purpose of the Study:
- To develop a structural model of the leptin-receptor complex.
- To utilize structural similarities with the G-CSF/G-CSF receptor complex for modeling.
- To provide a basis for experimental studies on leptin-receptor interactions.
Main Methods:
- Homology modeling was employed using the G-CSF/G-CSF receptor complex as a template.
- The crystal structure of the G-CSF/G-CSF receptor complex served as the structural basis.
- The generated model was validated against experimental data.
Main Results:
- A model structure for the leptin-receptor complex was successfully generated.
- The computational model demonstrated consistency with amino acid mutation and deletion experiments.
- The model provides insights into the atomic interactions between leptin and its receptor.
Conclusions:
- The developed model is a valuable tool for guiding future experimental research.
- The model supports further investigation into the leptin signaling pathway.
- This structural model facilitates a deeper understanding of leptin's biological functions.
Related Concept Videos
Ligand Binding Sites
Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
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 analyses the...
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 analyses the...
Assembly 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,...
G 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...
The 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...
Insulin: The Receptor and Signaling Pathways
Insulin action is mediated through a receptor tyrosine kinase, akin to the IGF-1 receptor. The number of receptors per cell varies significantly, from 40 on erythrocytes to 300,000 on adipocytes and hepatocytes. The insulin receptor consists of linked α/β subunit dimers, forming a heterotetramer glycoprotein with two extracellular α subunits and two β subunits spanning the membrane. The α subunits inhibit the inherent tyrosine kinase activity of the β subunits, but this inhibition is released...

