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Related Concept Videos

Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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,...
Cytoskeletal Linker Proteins - Plakins01:09

Cytoskeletal Linker Proteins - Plakins

Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...
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...

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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Protein assemblies with palindromic structure motifs.

N Pinotsis1, M Wilmanns

  • 1EMBL Hamburg, Notkestrasse 85, D-22603, Hamburg, Germany.

Cellular and Molecular Life Sciences : CMLS
|September 16, 2008
PubMed
Summary
This summary is machine-generated.

Recent discoveries reveal palindromic protein/protein complexes formed by symmetric sequence motifs. These complexes exhibit palindromic symmetry, arising from adjacent or remote, repeated, or inverted sequence elements.

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Area of Science:

  • Structural biology
  • Biochemistry
  • Molecular genetics

Background:

  • Symmetric DNA motifs enable palindromic protein/DNA complexes.
  • Symmetric protein motifs are less common but increasingly recognized.

Purpose of the Study:

  • To review and comment on recent findings concerning palindromic protein/protein complexes.
  • To highlight the structural basis and formation mechanisms of these symmetric complexes.

Main Methods:

  • Literature review of recent structural discoveries.
  • Analysis of sequence and structural data for palindromic protein complexes.

Main Results:

  • Identified palindromic protein/protein complexes with varying symmetry origins.
  • Demonstrated that symmetry can arise from adjacent or remote, repeated or inverted sequence motifs.
  • Highlighted the structural diversity in the formation of these complexes.

Conclusions:

  • Palindromic symmetry in protein/protein complexes, though less common than in DNA complexes, is structurally diverse.
  • Recent findings expand our understanding of how protein sequence symmetry dictates complex formation and architecture.