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

Proteinase-protein inhibitor interaction.

W Bode1, R Huber

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

Biomedica Biochimica Acta
|January 1, 1991
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

Crystallographic and kinetic investigations on the mechanism of 6-pyruvoyl tetrahydropterin synthase.

Journal of molecular biology·1999
Same author

Structural analysis at 2.2 A of orthorhombic crystals presents the asymmetry of the allophycocyanin-linker complex, AP.LC7.8, from phycobilisomes of Mastigocladus laminosus.

Proceedings of the National Academy of Sciences of the United States of America·1999
Same author

The 2.2 A crystal structure of human chymase in complex with succinyl-Ala-Ala-Pro-Phe-chloromethylketone: structural explanation for its dipeptidyl carboxypeptidase specificity.

Journal of molecular biology·1999
Same author

Glypican 3 and glypican 4 are juxtaposed in Xq26.1.

Gene·1999
Same author

Crystal structure of L-arginine:inosamine-phosphate amidinotransferase StrB1 from Streptomyces griseus: an enzyme involved in streptomycin biosynthesis.

Biochemistry·1999
Same author

The ligand-induced structural changes of human L-Arginine:Glycine amidinotransferase. A mutational and crystallographic study.

The Journal of biological chemistry·1999

Protein inhibitor-proteinase interactions were previously modeled as substrate-like or product-like. New structural studies reveal novel, partially substrate-like interaction modes, though serpin mechanisms remain unclear.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Traditional models for protein inhibitor-proteinase interactions include substrate-like inhibition by small serine proteinase inhibitors and product-like inhibition by carboxypeptidase inhibitors.
  • These models were the primary framework for understanding protein-proteinase dynamics for an extended period.

Purpose of the Study:

  • To explore novel modes of protein inhibitor-proteinase interactions beyond established models.
  • To investigate the structural basis of these interactions using recently determined complex structures.
  • To clarify the ongoing mechanistic questions surrounding serpin-proteinase interactions.

Main Methods:

  • Analysis of recently published complex structures, specifically cystatin/stefin-papain and hirudin-thrombin complexes.

Related Experiment Videos

  • Comparison of observed interaction modes with existing canonical and product-like inhibition models.
  • Review of current understanding and remaining conjectures regarding serpin mechanisms.

    • Main Results:

    • Novel interaction modes, exhibiting only partial substrate-like characteristics, have been identified in cystatin/stefin-papain and hirudin-thrombin complexes.
    • These findings challenge the exclusivity of previously established substrate-like and product-like inhibition models.
    • Despite advances in understanding serpin conformational changes, their precise inhibitory mechanisms against target serine proteinases remain largely speculative.

    Conclusions:

    • Protein inhibitor-proteinase interactions are more diverse than previously assumed, incorporating novel, partially substrate-like modes.
    • Structural insights into complexes like cystatin-papain and hirudin-thrombin are crucial for redefining interaction paradigms.
    • Further research is needed to elucidate the complex mechanisms of serpin inhibition, which continue to be an area of active investigation.