protein folding chaperone complex

Definition

Target type: cellularcomponent

A protein complex required for the non-covalent folding or unfolding, maturation, stabilization or assembly or disassembly of macromolecular structures. Usually active during or immediately after completion of translation. Many chaperone complexes contain heat shock proteins. [GOC:bhm, PMID:21855797]

Protein folding chaperone complexes are multi-protein assemblies that assist in the proper folding of newly synthesized proteins. They are essential for cellular function, as misfolded proteins can be detrimental to cell survival. These complexes often reside in specific cellular compartments, reflecting the spatial organization of protein folding processes.

**Chaperonin Complexes:**

* **Location:** The most well-known chaperonin complexes are found in the cytoplasm and the mitochondria of eukaryotic cells.
* **Structure:** They typically consist of two stacked rings, each composed of multiple subunits.
* **Function:** These complexes provide a protected environment for protein folding, preventing aggregation and allowing the protein to fold correctly.

**Hsp70 Complexes:**

* **Location:** Found in the cytoplasm, endoplasmic reticulum (ER), and mitochondria.
* **Structure:** Typically consist of two domains: an ATPase domain and a substrate-binding domain.
* **Function:** These complexes bind to unfolded or misfolded proteins, preventing aggregation and promoting proper folding.

**Hsp90 Complexes:**

* **Location:** Found in the cytoplasm and nucleus.
* **Structure:** Typically dimeric proteins with two domains: an N-terminal ATPase domain and a C-terminal dimerization domain.
* **Function:** These complexes play crucial roles in regulating the folding and activation of a wide range of client proteins, including kinases, transcription factors, and steroid hormone receptors.

**Other Chaperone Complexes:**

* **ER chaperone complexes:** These include proteins like calnexin and calreticulin, which are essential for folding newly synthesized proteins in the ER lumen.
* **Mitochondrial chaperone complexes:** These include chaperones like Hsp60 and Hsp10, which are involved in the import and folding of proteins within the mitochondria.

**Overall, the cellular component of protein folding chaperone complexes is diverse and highly dynamic. These complexes are essential for maintaining cellular homeostasis by ensuring the proper folding of newly synthesized proteins and preventing the accumulation of misfolded proteins. The specific composition and location of these complexes vary depending on the cellular compartment and the type of protein being folded.**'
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Proteins (6)

Compounds (65)