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Related Concept Videos

Conservation of Protein Domains Over Different Proteins02:26

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...
Conservation of Protein Domains02:26

Conservation of Protein Domains

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...
Multi-species Conserved Sequences02:51

Multi-species Conserved Sequences

Next-generation sequencing technologies have created large genomic databases of a variety of animals and plants. Ever since the human genome project was completed, scientists studied the genome of primates, mammals, and other phylogenetically distant living beings. Such large-scale  studies have provided new insights into the evolutionary relationship between organisms.
Although the genome of each species varies greatly from each other, a few sequences are highly conserved. Such conserved DNA...
Conserved Binding Sites01:49

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...
Conserved Binding Sites01:49

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 Families02:47

Protein Families

Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key locations, protein...

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Related Experiment Video

Updated: Jun 4, 2026

Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications
09:29

Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications

Published on: May 18, 2017

Conservation of Human IgSF Proteins Throughout Eukaryotic Evolution.

Steven Grudman1,2, Andras Fiser1,2

  • 1Department of Systems & Computational Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA.

Genome Biology and Evolution
|June 2, 2026
PubMed
Summary

The human immunoglobulin superfamily (IgSF) evolved across six major timeframes, influencing immune regulation and cell adhesion. This study maps IgSF evolution, revealing functional adaptations tied to new physiological systems.

Keywords:
evolution of adaptive immune systemevolution of co-stimulatory immune receptorsextracellular IgSFgnathostomes

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Related Experiment Videos

Last Updated: Jun 4, 2026

Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications
09:29

Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications

Published on: May 18, 2017

An Integrated Approach for Microprotein Identification and Sequence Analysis
09:37

An Integrated Approach for Microprotein Identification and Sequence Analysis

Published on: July 12, 2022

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

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

Published on: July 14, 2015

Area of Science:

  • Evolutionary Biology
  • Immunology
  • Genomics

Background:

  • The human immunoglobulin superfamily (IgSF) comprises numerous proteins crucial for cell adhesion, neural development, and immune regulation.
  • Many IgSF proteins function as key checkpoint proteins in biological processes.

Purpose of the Study:

  • To systematically analyze eukaryotic genomes and determine the evolutionary emergence of human IgSF subfamilies.
  • To establish an evolutionary framework for organizing the human IgSF by ancestry and function.

Main Methods:

  • Systematic analysis of all available eukaryotic reference genomes.
  • Partitioning IgSFs into six major evolutionary timeframes (Metazoa, Vertebrata, Gnathostomata, Tetrapoda, Amniota, Mammalia).
  • Conservation and functional analyses of IgSF proteins.

Main Results:

  • IgSFs emerged across six distinct evolutionary periods, correlating with the development of new physiological systems.
  • IgSFs appearing in tetrapods and amniotes primarily regulate immune responses and form immune synapse components.
  • Mammalian IgSF genes fine-tune immune activation for maternal-fetal tolerance.

Conclusions:

  • The study provides a framework for understanding IgSF evolution and function.
  • Identifies conserved, understudied IgSF proteins that emerged with the adaptive immune system as candidates for future research.
  • Highlights functional convergence and compensatory evolution within IgSF families.