Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Thrombin allostery.

Enrico Di Cera1, Michael J Page, Alaji Bah

  • 1Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110, USA. enrico@wustl.edu

Physical Chemistry Chemical Physics : PCCP
|March 10, 2007
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

The folding pathway of prothrombin.

Journal of thrombosis and haemostasis : JTH·2026
Same author

Cryogenic electron microscopy and coagulation factors.

Current opinion in hematology·2026
Same author

Molecular mechanism of cleavage at R271 during prothrombin activation revealed by cryo-EM.

Blood·2026
Same author

Lipoengineering of Biomolecular Condensates Controls Material Properties and Multiphase Hierarchy to Guide Organoid Morphogenesis.

bioRxiv : the preprint server for biology·2026
Same author

Structural determinants of protease-activated receptor 1 cleavage by activated protein C.

Journal of thrombosis and haemostasis : JTH·2025
Same author

Uncovering the Molecular Interactions Underlying MBD2 and MBD3 Phase Separation.

The journal of physical chemistry. B·2025
Same journal

Stability constants of lanthanide-nitrate complexes in aqueous solutions: a theoretical study.

Physical chemistry chemical physics : PCCP·2026
Same journal

Lead-free Cs<sub>3</sub>MnCl<sub>5</sub> and CsMnCl<sub>3</sub> crystals: rapid on-chip crystallization, phase transition and fluorescence sensing applications.

Physical chemistry chemical physics : PCCP·2026
Same journal

F-Interstitial passivation preserves host-like optoelectronic properties in <sup>229</sup>Th:YLF nuclear-clock platforms.

Physical chemistry chemical physics : PCCP·2026
Same journal

Structural trends of tryptophan dimer: hydrogen bonding <i>versus</i> π-stacking from an energy decomposition analysis perspective.

Physical chemistry chemical physics : PCCP·2026
Same journal

Achieving high thermoelectric performance in Sb<sub>2</sub>Se<sub>3</sub>-alloyed GeTe through synergistic optimization of electrical and thermal transport.

Physical chemistry chemical physics : PCCP·2026
Same journal

Ultraviolet perfect absorption leveraging bound states in the continuum in an Al/SiO<sub>2</sub> hybrid system.

Physical chemistry chemical physics : PCCP·2026
See all related articles

Sodium ions (Na(+)) activate thrombin, a key enzyme in blood clotting. Understanding this allosteric activation mechanism reveals insights into blood pathophysiology and enzyme function.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Hematology

Background:

  • Thrombin is a critical serine protease involved in blood coagulation and pathophysiology.
  • Sodium ion (Na(+)) binding is essential for thrombin's procoagulant, prothrombotic, and signaling functions.
  • Thrombin's allosteric regulation by Na(+) is a key determinant of its diverse roles.

Purpose of the Study:

  • To review the current understanding of the molecular basis of thrombin allostery.
  • To emphasize the kinetic aspects of Na(+) activation in thrombin.
  • To highlight thrombin allostery as a model for long-range communication in biological systems.

Main Methods:

  • Literature review of existing research on thrombin structure and function.
  • Analysis of kinetic data related to sodium ion binding.

Related Experiment Videos

  • Molecular modeling and simulation studies (implied).

    • Main Results:

    • Na(+) binding induces conformational changes in thrombin, modulating its activity.
    • Allosteric effects of Na(+) are crucial for thrombin's physiological and pathological functions.
    • The mechanism of Na(+) activation involves long-range communication within the thrombin molecule.

    Conclusions:

    • Thrombin allostery, particularly Na(+) activation, is fundamental to blood pathophysiology.
    • Understanding thrombin's kinetic and molecular mechanisms provides insights into enzyme regulation.
    • Thrombin serves as a paradigm for studying allosteric regulation and signal transmission in other enzymes.