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

Endoproteinase-protein inhibitor interactions.

W Bode1, C Fernandez-Catalan, H Nagase

  • 1Max-Planck-Institut für Biochemie, Martinsried, Germany.

APMIS : Acta Pathologica, Microbiologica, Et Immunologica Scandinavica
|April 6, 1999
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

Structural basis for possible calcium-induced activation mechanisms of calpains.

Biological chemistry·2001
Same author

Glucocorticoids preferentially upregulate functional CXCR4 expression in eosinophils.

The Journal of allergy and clinical immunology·2000
Same author

Activation of G-proteins in the mouse pons/medulla by beta-endorphin is mediated by the stimulation of mu- and putative epsilon-receptors.

Life sciences·2000
Same author

Differential involvement of mu(1)-opioid receptors in endomorphin- and beta-endorphin-induced G-protein activation in the mouse pons/medulla.

Neuroscience·2000
Same author

Significance of coexpression of urokinase-type plasminogen activator, and matrix metalloproteinase 3 (stromelysin) and 9 (gelatinase B) in colorectal carcinoma.

The Journal of surgical research·2000
Same author

Alleviation of renal disease and lymphadenopathy in MRL-Fasp(lrcg)/Fas(lprcg) (MR-lpr(cg)) mice neonatally infected with mouse mammary tumor virus encoding superantigen strongly reactive with TCR Vbeta8.2 element.

Viral immunology·2000

Protein inhibitors regulate proteinase activity. This study explores canonical and non-canonical binding mechanisms, focusing on matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) interactions.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Protein inhibitors are crucial for regulating proteinase activity in biological systems.
  • Canonical inhibitors typically bind serine proteinases via substrate-like interactions.
  • Emerging research reveals non-canonical inhibition mechanisms.

Purpose of the Study:

  • To review diverse proteinase inhibitor binding modes.
  • To highlight novel inhibition mechanisms beyond canonical interactions.
  • To emphasize the structural basis of matrix metalloproteinase (MMP) inhibition by tissue inhibitors of metalloproteinases (TIMPs).

Main Methods:

  • Analysis of existing 3D structural data for various proteinase inhibitors.
  • Comparison of canonical and non-canonical inhibitor-proteinase interactions.

Related Experiment Videos

  • Focus on structural characterization of MMP-TIMP complexes.

    • Main Results:

    • Most characterized inhibitors exhibit canonical binding to serine proteinases.
    • Non-canonical inhibitors, cysteine proteinase inhibitors, and zinc endopeptidase inhibitors display varied interaction modes.
    • Detailed structural insights into MMP-TIMP interactions reveal specific inhibition strategies.

    Conclusions:

    • Proteinase inhibition involves diverse structural mechanisms.
    • Non-canonical interactions represent an expanding area of inhibitor research.
    • Understanding MMP-TIMP interactions is key to comprehending metalloproteinase regulation.