Related Experiment Video

Updated: Jun 19, 2026

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein
11:23

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Published on: June 30, 2019

Structural basis for the inhibitor recognition of human Lyn kinase domain

Nao Miyano1, Takayoshi Kinoshita, Ryoko Nakai

  • 1Graduate School of Science, Osaka Prefecture University, Sakai, Osaka 599-8531, Japan.

Bioorganic & Medicinal Chemistry Letters
|October 28, 2009
PubMed

Insights

Human Lyn tyrosine kinase, crucial for immune signaling, is implicated in tumors. Staurosporine binding reveals structural insights for designing new Lyn-specific cancer inhibitors.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Human Lyn tyrosine kinase is vital for hematopoietic immune system signal transduction.
  • Aberrant Lyn kinase activity is linked to the development of various cancers.

Purpose of the Study:

  • To investigate the structural basis of staurosporine inhibition of human Lyn kinase.
  • To provide insights for the rational design of novel Lyn-selective inhibitors.

Main Methods:

  • X-ray crystallography was used to determine the structure of human Lyn kinase.
  • Analysis of the staurosporine-binding site within the Lyn kinase domain.

Main Results:

  • The crystal structure revealed that staurosporine binds to the ATP-binding site of human Lyn kinase.
  • Key structural features of the staurosporine-binding region were identified.

Conclusions:

  • The identified structural features offer valuable insights for structure-based drug design.
  • This study facilitates the development of novel, Lyn-selective inhibitors for therapeutic applications.

More Related Videos

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors10:33

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

Published on: October 26, 2015

A Guide to Production, Crystallization, and Structure Determination of Human IKK1/α11:27

A Guide to Production, Crystallization, and Structure Determination of Human IKK1/α

Published on: November 2, 2018

Related Concept Videos

Enzymes02:34

Enzymes

Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
Receptor Tyrosine Kinases01:26

Receptor Tyrosine Kinases

Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
Enzyme Inhibition01:30

Enzyme Inhibition

Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.
Ligand Binding Sites02:40

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...