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 Concept Videos

G Protein-coupled Receptors01:15

G Protein-coupled Receptors

G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Selectins01:25

Selectins

Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain, which...
Activation of Integrins01:15

Activation of Integrins

Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

High-throughput in situ single particle X-ray imaging of dehydrating viral capsids.

Light, science & applications·2026
Same author

Molecular mechanisms of transhydrogenase activity and allosteric regulation in eukaryotic type II PHGDH Ser33.

Nature communications·2026
Same author

Revisiting the life cycle of temperate phages.

Nature reviews. Microbiology·2026
Same author

Structural basis for phosphorylation and allosteric regulation of bacterial glycogen phosphorylase by histidine phosphocarrier protein.

Nature communications·2026
Same author

Engineering Penicillium expansum antifungal proteins unveils new clues about their mode of action.

Applied microbiology and biotechnology·2026
Same author

Phages communicate across species to shape microbial ecosystems.

Cell·2026

Related Experiment Video

Updated: May 24, 2026

Identification of Functional Protein Regions Through Chimeric Protein Construction
11:39

Identification of Functional Protein Regions Through Chimeric Protein Construction

Published on: January 8, 2019

Structural and functional insights into endoglin ligand recognition and binding.

Aaron Alt1, Laura Miguel-Romero, Jordi Donderis

  • 1Instituto de Biomedicina de Valencia, Valencia, Spain.

Plos One
|February 21, 2012
PubMed
Summary
This summary is machine-generated.

Endoglin

More Related Videos

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

Related Experiment Videos

Last Updated: May 24, 2026

Identification of Functional Protein Regions Through Chimeric Protein Construction
11:39

Identification of Functional Protein Regions Through Chimeric Protein Construction

Published on: January 8, 2019

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

Area of Science:

  • Molecular and Cellular Biology
  • Biochemistry
  • Structural Biology

Background:

  • Endoglin is a glycoprotein in the transforming growth factor (TGF)-β receptor complex, crucial for vascular endothelial cells.
  • It is linked to hereditary hemorrhagic telangiectasia and preeclampsia.
  • Endoglin interacts with activin receptor-like kinase (ALK)1 and modulates responses to Bone Morphogenetic Proteins (BMPs).

Purpose of the Study:

  • To investigate the binding interactions between endoglin, ALK1, and BMP-9.
  • To identify the specific domain of endoglin responsible for BMP-9 recognition.
  • To characterize the structural properties of endoglin domains.

Main Methods:

  • Surface plasmon resonance (SPR) assays to measure binding kinetics.
  • Cellular assays to assess functional interactions.
  • Small-angle X-ray scattering (SAXS) to determine structural conformation.

Main Results:

  • Endoglin and ALK1 ectodomains bind independently to distinct sites on BMP-9.
  • The endoglin orphan domain (OD) (residues 22-337) is the minimal domain for BMP-9 binding.
  • Cysteine 350 (Cys350) is critical for endoglin dimerization; the OD is monomeric.

Conclusions:

  • The orphan domain of endoglin is essential for its interaction with BMP-9.
  • Endoglin's binding to BMP-9 is independent of glycosylation and cooperativity.
  • Structural characterization reveals a compact conformation of the endoglin OD.