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

I-type lectins.

Takashi Angata1, Els Brinkman-Van der Linden

  • 1Glycobiology Research and Training Center, University of California, San Diego, 9500 Gilman Drive, 0687, La Jolla CA 92093-0687, USA. tangata@ucsd.edu

Biochimica Et Biophysica Acta
|September 12, 2002
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

Carbohydrate sulfotransferases in humans: Repertoire and regulation of glycan-lectin interactions.

Biochimica et biophysica acta. General subjects·2026
Same author

Comprehensive identification of the genes involved in the expression of Siglec-15 ligands on osteoclast precursors.

Cell reports·2026
Same author

Insights into the transcriptional regulation of CD22 in B cell chronic lymphocytic leukemia.

The Journal of biological chemistry·2025
Same author

Comprehensive Modular Synthesis of Ganglioside Glycans and Evaluation of their Binding Affinities to Siglec-7 and Siglec-9.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2024
Same author

B4GALT1-dependent galectin-8 binding with TGF-β receptor suppresses colorectal cancer progression and metastasis.

Cell death & disease·2024
Same author

Functional and structural investigation of a broadly neutralizing SARS-CoV-2 antibody.

JCI insight·2024
Same journal

Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

Molecular Basis of Disease Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

General Subjects Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

Erratum to 'on the role of exchangeable hydrogen bonds for the kinetics of P680<sup>+·</sup> Q<sub>A</sub> <sup>-·</sup> formation and P680<sup>+·</sup> Pheo<sup>-·</sup> recombination in photosystem II' [Biochim. Biophys. Acta 1276 (1996) 35-44].

Biochimica et biophysica acta·2019
Same journal

Oligomeric state of the light-harvesting complexes B800-850 and B875 from purple bacterium Rubrivivax gelatinosus in detergent solution.

Biochimica et biophysica acta·2019
Same journal

Regulation of pigment content and enzyme activity in the cyanobacterium Nostoc sp. Mac grown in continuous light, a light-dark photoperiod, or darkness.

Biochimica et biophysica acta·2019
See all related articles

The immunoglobulin superfamily includes I-type lectins, which bind carbohydrates. This review covers their occurrence, structure, binding, and functions.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Immunology

Background:

  • The immunoglobulin superfamily is a large protein group characterized by structural similarity to immunoglobulins.
  • Most superfamily proteins function in protein-protein interactions, acting as receptors, antibodies, or cell adhesion molecules.
  • I-type lectins are a distinct subset within this superfamily, specialized for carbohydrate-protein interactions.

Purpose of the Study:

  • To review the occurrence, structure, binding properties, and potential biological functions of I-type lectins.
  • To highlight the role of I-type lectins in recognizing various carbohydrates, including sialic acids, other sugars, and glycosaminoglycans.

Main Methods:

  • Literature review and synthesis of existing research on I-type lectins.

Related Experiment Videos

  • Analysis of structural data and binding characteristics of I-type lectins.
  • Compilation of information on the known and proposed biological roles of these lectins.

    • Main Results:

    • I-type lectins exhibit diverse carbohydrate-binding specificities, recognizing sialic acids, other neutral and acidic sugars, and glycosaminoglycans.
    • These lectins are found across various species and biological contexts, suggesting broad functional importance.
    • Their structural features within the immunoglobulin fold enable specific molecular recognition of carbohydrate structures.

    Conclusions:

    • I-type lectins represent a significant group of carbohydrate-binding proteins within the immunoglobulin superfamily.
    • Understanding their diverse binding properties and functions is crucial for deciphering their roles in biological processes.
    • Further research into I-type lectin functions could reveal new therapeutic targets and diagnostic tools.