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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...
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...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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 to...
Membrane Domains01:18

Membrane Domains

The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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 to...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...

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Mathematical modeling of the dynamic mechanical behavior of neighboring sarcomeres in actin stress fibers.

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LIM proteins in actin cytoskeleton mechanoresponse.

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91st annual meeting of the American Association for Cancer Research.

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Related Experiment Video

Updated: Jun 4, 2026

Lipid Vesicle-mediated Affinity Chromatography using Magnetic Activated Cell Sorting (LIMACS): a Novel Method to Analyze Protein-lipid Interaction
07:33

Lipid Vesicle-mediated Affinity Chromatography using Magnetic Activated Cell Sorting (LIMACS): a Novel Method to Analyze Protein-lipid Interaction

Published on: April 26, 2011

The LIM domain is a modular protein-binding interface

K L Schmeichel1, M C Beckerle

  • 1Biology Department, University of Utah, Salt Lake City 84112.

Cell
|October 21, 1994
PubMed
Summary

LIM domains are essential zinc-binding protein sequences. Studies show a specific LIM domain in zyxin protein is crucial for binding to its partner, cysteine-rich protein (CRP), revealing its role in protein interactions.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • LIM domains are conserved zinc-binding motifs present in various proteins.
  • These proteins include transcriptional regulators, proto-oncogenes, and components of adhesion plaques.
  • Zyxin is an adhesion plaque protein characterized by three C-terminal LIM domains.

Purpose of the Study:

  • To define the biological activity and function of LIM domains.
  • To investigate the role of LIM domains in protein-protein interactions using zyxin as a model.
  • To identify the specific LIM domain(s) responsible for zyxin's interactions with binding partners.

Main Methods:

  • Reconstitution of protein complexes involving zyxin and its binding partners, alpha-actinin and cysteine-rich protein (CRP).

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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

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein
11:23

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Published on: June 30, 2019

Related Experiment Videos

Last Updated: Jun 4, 2026

Lipid Vesicle-mediated Affinity Chromatography using Magnetic Activated Cell Sorting (LIMACS): a Novel Method to Analyze Protein-lipid Interaction
07:33

Lipid Vesicle-mediated Affinity Chromatography using Magnetic Activated Cell Sorting (LIMACS): a Novel Method to Analyze Protein-lipid Interaction

Published on: April 26, 2011

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

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein
11:23

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Published on: June 30, 2019

  • Analysis of protein-protein interactions mediated by zyxin's LIM domains.
  • Functional assays to determine necessity and sufficiency of individual LIM domains for binding.

    • Main Results:

    • One of the three C-terminal LIM domains of zyxin is essential for its association with CRP.
    • This specific LIM domain is both necessary and sufficient to mediate the zyxin-CRP interaction.
    • The study provides direct evidence for the LIM domain acting as a protein-binding interface.

    Conclusions:

    • LIM domains function as specific protein-binding interfaces.
    • The findings elucidate the molecular mechanism by which zyxin interacts with CRP.
    • This research contributes to understanding the broader role of LIM domains in cellular processes and protein complex formation.