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

Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

6.2K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
6.2K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.7K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.7K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

8.2K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
8.2K
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

46.1K
Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
46.1K

You might also read

Related Articles

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

Sort by
Same author

Ultraslow conformational dynamics and catch bond formation of a bacterial adhesin revealed by a single-domain variant of FimH.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Pharmacologic glycoengineering of Fcγ receptor IIIa enhances force-resistant IgG-FcγR interactions and anti-tumor antibody efficacy.

Immunity·2026
Same author

Correction: Toggle switch residues control allosteric transitions in bacterial adhesins by participating in a concerted repacking of the protein core.

PLoS pathogens·2026
Same author

Antibodies disrupt bacterial adhesion by ligand mimicry and allosteric interference.

Nature communications·2025
Same author

<i>De Novo</i> Design of Miniprotein Inhibitors of Bacterial Adhesins.

bioRxiv : the preprint server for biology·2025
Same author

Ultra-slow conformational dynamics and catch bond formation of a Bacterial Adhesin revealed by a single-domain variant of FimH.

bioRxiv : the preprint server for biology·2025

Related Experiment Video

Updated: Nov 21, 2025

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
08:53

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro

Published on: January 11, 2017

9.2K

FimH as a scaffold for regulated molecular recognition.

Shivani Gupta Ludwig1, Casey L Kiyohara1, Laura A Carlucci1

  • 1Department of Bioengineering, University of Washington, 3720 15th Ave NE. Foege N430P, Box 355061, Seattle, USA.

Journal of Biological Engineering
|January 13, 2021
PubMed
Summary

Researchers engineered the bacterial FimH protein to create regulated molecular recognition. This scaffold maintains conformation-dependent binding, enabling tunable affinity for new targets like Penta-His antibody through allosteric and parasteric mechanisms.

Keywords:
AllosteryConformational changeFimHParastericRecognition moleculesRegulation

More Related Videos

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy
11:13

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

Published on: August 20, 2018

11.4K
High Precision FRET at Single-molecule Level for Biomolecule Structure Determination
11:24

High Precision FRET at Single-molecule Level for Biomolecule Structure Determination

Published on: May 13, 2017

11.0K

Related Experiment Videos

Last Updated: Nov 21, 2025

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
08:53

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro

Published on: January 11, 2017

9.2K
Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy
11:13

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

Published on: August 20, 2018

11.4K
High Precision FRET at Single-molecule Level for Biomolecule Structure Determination
11:24

High Precision FRET at Single-molecule Level for Biomolecule Structure Determination

Published on: May 13, 2017

11.0K

Area of Science:

  • Biotechnology
  • Protein Engineering
  • Molecular Recognition

Background:

  • Antibodies are the standard for molecular recognition but lack convenient regulation.
  • Alternative protein scaffolds offer opportunities for novel functionalities, including regulated binding.
  • The bacterial adhesin FimH exhibits conformation-dependent binding to mannose, regulated by allosteric and parasteric mechanisms.

Purpose of the Study:

  • To investigate FimH as a scaffold for regulated molecular recognition.
  • To determine if FimH's conformational regulation is retained after altering its binding site.
  • To explore the utility of FimH's native regulatory mechanisms for new targets.

Main Methods:

  • Reengineering the FimH binding site to recognize non-mannosylated targets (nickel, Penta-His antibody).
  • Assessing changes in binding affinity (KD) between different FimH conformations.
  • Utilizing allosteric and parasteric regulation with native ligands and antibodies to modulate binding.

Main Results:

  • Engineered FimH variants maintained conformational regulation, showing up to a 7-fold difference in KD for new targets.
  • Both allosteric and parasteric mechanisms successfully regulated binding to Penta-His antibody.
  • Allosteric regulation by mab21 reduced affinity 7-fold, inducing 98% target detachment.

Conclusions:

  • FimH serves as a versatile scaffold for developing conformationally regulated binding proteins.
  • The deeply studied, conformation-dependent binding of FimH can be adapted for multiple regulatory strategies.
  • This approach offers potential for advanced biotechnology applications requiring tunable molecular recognition.