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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

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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...
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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.
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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.
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A Protocol for Computer-Based Protein Structure and Function Prediction
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A Web-Based Protocol for Interprotein Contact Prediction by Deep Learning.

Xiaoyang Jing1,2, Hong Zeng3, Sheng Wang1

  • 1Toyota Technological Institute at Chicago, Chicago, IL, USA.

Methods in Molecular Biology (Clifton, N.J.)
|October 5, 2019
PubMed
Summary
This summary is machine-generated.

Predicting protein-protein contacts is vital for cell function. RaptorX-ComplexContact, a new deep learning web server, accurately identifies these contacts using paired protein sequence alignments and neural networks.

Keywords:
Deep learning (DL)Direct-coupling analysis (DCA)Interprotein contact predictionMultiple sequence alignment (MSA)Protein complexProtein dockingProtein interaction networkProtein–protein interaction (PPI) prediction

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Area of Science:

  • Biochemistry and Molecular Biology
  • Computational Biology
  • Bioinformatics

Background:

  • Accurate identification of residue-residue contacts in protein-protein interactions is essential for understanding protein function and cellular mechanisms.
  • Existing methods like direct-coupling analysis (DCA) require numerous sequence homologs for reliable predictions, limiting their applicability.

Purpose of the Study:

  • To develop an advanced computational tool for predicting interprotein residue-residue contacts.
  • To leverage deep learning for improved accuracy in contact prediction compared to traditional methods.

Main Methods:

  • Developed RaptorX-ComplexContact, a web server utilizing deep convolutional residual neural networks (ResNet).
  • Constructed paired multiple sequence alignments (MSAs) using genomic distance and phylogenetic information from sequence homologs.
  • Integrated sequential features and coevolutionary information from paired MSAs for contact prediction.

Main Results:

  • RaptorX-ComplexContact demonstrates effective prediction of interprotein residue-residue contacts.
  • The method utilizes deep learning architectures for enhanced prediction accuracy.

Conclusions:

  • RaptorX-ComplexContact provides a valuable resource for predicting interprotein contacts.
  • This tool can significantly aid in protein docking, protein-protein interaction prediction, and the construction of protein interaction networks.