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Protein Complex Assembly

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 Assembly

Protein Complex Assembly

Assembly of Signaling Complexes

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,...

Assembly of Cytoskeletal Filaments

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...

Protein Complexes with Interchangeable Parts

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...

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

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Updated: Apr 27, 2026

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

Design and designability of protein-based assemblies.

Jian Zhang¹, Fan Zheng², Gevorg Grigoryan³

¹Department of Computer Science, Dartmouth College, Hanover, NH, USA.

Current Opinion in Structural Biology

|June 22, 2014

Summary

Designing protein assemblies is advancing molecular engineering. Successful designs share a key property: natural designability, meaning they work well with various amino acid sequences.

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Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

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Area of Science:

Molecular Engineering
Protein Design
Supramolecular Chemistry

Background:

Protein-based assembly design is a growing field in molecular engineering.
Current approaches often involve patterning existing protein units to create diverse geometries, utilizing symmetry for lattices and particles.
Key challenges include specificity and folding problems.

Purpose of the Study:

To review recent advancements in protein assembly design.
To identify commonalities in successful design strategies.
To address the specificity and folding challenges in designing protein superstructures.

Main Methods:

Analysis of recent results in protein assembly design.
Focus on strategies addressing specificity and folding problems.
Identification of unifying properties in successful designs.

Main Results:

Successful protein assembly designs often exhibit natural designability.
Natural designability refers to the compatibility of assembly elements with diverse natural amino acid sequences.
This property may be a unifying factor across various successful design approaches.

Conclusions:

Natural designability is a crucial property for successful protein assembly design.
Understanding and engineering this property can overcome key design challenges.
This insight advances the field of molecular engineering and protein design.