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

A logical sequence search for S100B target proteins.

K A McClintock1, G S Shaw

  • 1Department of Biochemistry and McLaughlin Macromolecular Structure Facility, The University of Western Ontario, London, Ontario, Canada.

Protein Science : a Publication of the Protein Society
|December 6, 2000
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

Identification of a molecular recognition feature in the E1A oncoprotein that binds the SUMO conjugase UBC9 and likely interferes with polySUMOylation.

Oncogene·2010
Same author

Structure of a conjugating enzyme-ubiquitin thiolester intermediate reveals a novel role for the ubiquitin tail.

Structure (London, England : 1993)·2001
Same author

Identification of the ubiquitin interfacial residues in a ubiquitin-E2 covalent complex.

Journal of biomolecular NMR·2001
Same author

The solution structure of the C-terminal domain of the Mu B transposition protein.

The EMBO journal·2000
Same author

Letter to the editor: 1H, 15N and 13C resonance assignments for the catalytic domain of the yeast E2, UBC1.

Journal of biomolecular NMR·2000
Same author

Sequence specific analysis of the heterogeneous glycan chain from peanut peroxidase by 1H-NMR spectroscopy.

Phytochemistry·2000
Same journal

Macromolecular crowding inhibits degradation of alpha-synuclein amyloid fibrils induced by cathepsins and MMP9.

Protein science : a publication of the Protein Society·2026
Same journal

Sequence-encoded differences in the conformational ensembles of CITED transcriptional activation domains impact coactivator binding.

Protein science : a publication of the Protein Society·2026
Same journal

The phospholipid biosynthesis enzyme PlsB contains three distinct domains for membrane association, lysophosphatidic acid synthesis, and dimerization.

Protein science : a publication of the Protein Society·2026
Same journal

Structural basis of ligand selectivity in FAD/NAD(P)H-dependent dehydrogenases: insights from trypanothione reductase and type II NADH dehydrogenase.

Protein science : a publication of the Protein Society·2026
Same journal

Achieving protease substrate-specific inhibition by mAb dual functional selections.

Protein science : a publication of the Protein Society·2026
Same journal

How important are quantum mechanical effects in controlling biological functions: Enzymes, electron transfer and bird navigation.

Protein science : a publication of the Protein Society·2026
See all related articles

The EF-hand calcium-binding protein S100B interacts with tubulin and intermediate filament proteins. This interaction is explained by conserved sequences that S100B binds to, inhibiting protein assembly.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • The EF-hand calcium-binding protein S100B is known to interact with various substrates in a calcium-dependent manner.
  • Identifying specific S100B target proteins is crucial for understanding its cellular functions.

Purpose of the Study:

  • To screen potential S100B target proteins for a conserved consensus sequence.
  • To correlate sequence conservation with known structural and functional properties of proteins.
  • To provide a mechanistic explanation for S100B's observed effects on protein oligomerization.

Main Methods:

  • Screening of potential S100B target proteins for a conserved consensus sequence across species.
  • Comparison of identified conserved regions with known structural and in vitro properties of candidate proteins.

Related Experiment Videos

  • Analysis of sequence matches in relation to protein structure and function.

    • Main Results:

    • Four oligomeric proteins were identified as potential S100B binding partners: tubulin (alpha and beta), glial fibrillary acidic protein (GFAP), desmin, and vimentin.
    • Conserved regions matching the S100B consensus sequence were found in type III intermediate filament proteins (GFAP, desmin, vimentin) within a coiled-coil (helix 2A) region.
    • In tubulin, matching sequences were located at the alpha beta tubulin interface.

    Conclusions:

    • The identified conserved sequences provide a structural basis for S100B interaction with tubulin and intermediate filament proteins.
    • These findings offer a logical explanation for the in vitro inhibition of oligomerization of these proteins by S100B.
    • The study highlights the importance of conserved motifs in mediating protein-protein interactions and functional regulation.