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Related Concept Videos

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR activation may...
Eukaryotic Transcription Inhibitors01:52

Eukaryotic Transcription Inhibitors

Certain biochemical processes, such as embryonic development and cell growth regulation, depend on the repression of specific genes. DNA binding proteins known as eukaryotic transcription inhibitors regulate the repression of gene expression in eukaryotes. The presence of these inhibitors at the required location and time in the cell is triggered by the presence of hormones and additional signals from other cells.
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Updated: Jun 29, 2026

Dextran Labeling and Uptake in Live and Functional Murine Cochlear Hair Cells
05:55

Dextran Labeling and Uptake in Live and Functional Murine Cochlear Hair Cells

Published on: February 8, 2020

Na+ binding to meizothrombin desF1.

M E Papaconstantinou1, P S Gandhi, Z Chen

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

Cellular and Molecular Life Sciences : CMLS
|October 16, 2008
PubMed
Summary
This summary is machine-generated.

This study reveals the first X-ray crystal structure of human meizothrombin, identifying a sodium (Na+) binding site similar to thrombin. This finding supports meizothrombin

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Last Updated: Jun 29, 2026

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05:55

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Published on: February 8, 2020

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09:52

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Published on: March 16, 2018

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Meizothrombin is the active intermediate of prothrombin, crucial for blood coagulation.
  • Emerging evidence suggests meizothrombin functions as a sodium (Na+)-activated enzyme, similar to thrombin.

Purpose of the Study:

  • To determine the first X-ray crystal structure of human meizothrombin desF1.
  • To investigate the structural basis and functional implications of Na+ activation in meizothrombin.

Main Methods:

  • X-ray crystallography of human meizothrombin desF1 complexed with PPACK at 2.1 A resolution.
  • Stopped-flow fluorescence measurements to analyze Na+ binding kinetics.

Main Results:

  • The crystal structure revealed a Na+ binding site architecturally identical to that of human thrombin.
  • Kinetic studies demonstrated a slow phase of Na+ binding, indicative of multiple conformational states in equilibrium (E*, E, and E:Na+).

Conclusions:

  • Meizothrombin desF1 possesses a Na+ binding site structurally conserved with thrombin.
  • The existence of multiple conformations in meizothrombin provides critical insights into the prothrombin activation pathway.