Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Conservation of Protein Domains Over Different Proteins

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...

Conserved Binding Sites

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...

Protein Folding

Protein Folding

Protein Organization

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.

Protein-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

Protein-Protein Interfaces

Protein-Protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

You might also read

Related Articles

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

Sort by

Same author

Regulatory mechanism of heme-regulated inhibitor through autophosphorylation-driven activation and heme-induced deactivation.

Journal of biochemistry·2026

Same author

Discovery of TCR-like antibodies to the KRAS G12D neoantigen via in silico-in vitro workflow.

Molecular therapy : the journal of the American Society of Gene Therapy·2026

Same author

Towards the International Conference on Biophysics and Biomedical Sciences: ICBBS 2026.

Biophysics and physicobiology·2026

Same author

Multistep receptor binding of the hepatitis B virus preS1 domain.

Nature communications·2026

Same author

Graphene oxide-based fluorescent biosensor for high-throughput screening to discover SARS-CoV-2 RdRp inhibitors.

Journal of materials chemistry. B·2026

Same author

Structural mapping of NTCP distinguishes its dual functionality as a hepatitis B virus receptor and bile acid transporter.

PLoS pathogens·2026

Search research articles

Related Experiment Video

Updated: Jul 18, 2026

Electronic Tongue Generating Continuous Recognition Patterns for Protein Analysis

Electronic Tongue Generating Continuous Recognition Patterns for Protein Analysis

Published on: September 16, 2014

Structural basis for protein recognition by B30.2/SPRY domains.

Jae-Sung Woo¹, Hye-Young Suh, Sam-Yong Park

¹Center for Biomolecular Recognition, Department of Life Sciences, Division of Molecular and Life Sciences, Pohang University of Science and Technology, Pohang, Kyungbuk, 790-784, Korea.

|December 26, 2006

Summary

Researchers crystalized the B30.2/SPRY domain of GUSTAVUS, revealing its preformed pocket that binds VASA peptides. This discovery identified a similar binding motif in Par-4, suggesting broad target recognition by B30.2/SPRY domains.

More Related Videos

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Related Experiment Videos

Last Updated: Jul 18, 2026

Electronic Tongue Generating Continuous Recognition Patterns for Protein Analysis

Electronic Tongue Generating Continuous Recognition Patterns for Protein Analysis

Published on: September 16, 2014

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Area of Science:

Structural biology
Molecular biology
Protein-protein interactions

Background:

B30.2/SPRY domains are crucial in various cellular functions, including cytokine signaling and viral restriction.
Understanding the molecular mechanisms of B30.2/SPRY domain interactions is key to elucidating their biological roles.

Purpose of the Study:

To determine the crystal structure of the GUSTAVUS B30.2/SPRY domain complexed with a VASA-derived peptide.
To elucidate the molecular basis of high-affinity protein recognition by B30.2/SPRY domains.

Main Methods:

X-ray crystallography to determine the structure of the GUSTAVUS B30.2/SPRY domain and VASA peptide complex.
Bioinformatic analysis to identify conserved structural features and potential binding motifs in other B30.2/SPRY domains.

Main Results:

The crystal structure revealed a conformationally rigid peptide-binding site with a preformed pocket.
High-affinity binding between GUSTAVUS and VASA is mediated by the Asp-Ile-Asn-Asn-Asn-Asn sequence interacting with the pocket.
A similar recognition motif (Glu-Leu-Asn-Asn-Asn-Leu) was identified in Par-4 for interaction with SSB-1, a GUSTAVUS homolog.

Conclusions:

B30.2/SPRY domains possess preformed pockets that facilitate specific, high-affinity interactions with target peptides.
The identified binding motif suggests that many B30.2/SPRY domains can recognize multiple protein targets through similar structural mechanisms.
This structural insight provides a foundation for understanding innate immunity and retroviral restriction mechanisms.