Molecular chaperones

proteins assisting in protein folding

thumb|Schematic diagram highlighting the role of HSP70 in pathologies. The protective intracellular HSP70 is decreased whereas the levels of inflammatory extracellular HSP70 is increased. This imbalance leads to disease progression. The 70 kilodalton heat shock proteins (Hsp70s or DnaK) are a family of conserved ubiquitously expressed heat shock proteins. Proteins with similar structure exist in virtually all living organisms and play crucial roles in the development of cancer, neurodegeneration, apoptosis, regulating sleep, and much more. Intracellularly localized Hsp70s are an important part

Calreticulin also known as calregulin, CRP55, CaBP3, calsequestrin-like protein, and endoplasmic reticulum resident protein 60 (ERp60) is a protein that in humans is encoded by the CALR gene.

Chaperonins, abbreviated Cpn, Cpn60, or HSP60, are a family of heat shock proteins that assist in the folding of newly synthesized proteins and refolding of misfolded proteins during stressful conditions such as high temperature. They are protein complexes consisting of about 16 protein subunits of ~60 kDa each. Chaperonins belong to a large class of molecules and complexes that assist protein folding, called molecular chaperones.

protein-coding gene in the species Homo sapiens

thumb|236px|Domain structure of the yeast heat-inducible Hsp90. Top: Crystallographic structure of the dimeric Hsp90. Bound ATP molecules are represented by space filling spheres. Bottom: 1D sequence of the yeast Hsp90. NTD= N-terminus|N-terminal domain (red), MD = middle domain (green), CTD = C-terminal domain (blue). thumb|236px|X-ray crystallography|Crystallographic structure of the ATP binding pocket of Hsp90 where ATP is represented by a ball and stick figure (carbon atoms = grey, nitrogen = blue, oxygen = red, phosphorus = orange) and Hsp90 is depicted as a solid surface (negatively char

Calnexin (CNX) is a 67kDa integral protein (that appears variously as a 90kDa, 80kDa, or 75kDa band on western blotting depending on the source of the antibody) of the endoplasmic reticulum (ER). It consists of a large (50 kDa) N-terminal calcium-binding lumenal domain, a single transmembrane helix and a short (90 residues), acidic cytoplasmic tail. In humans, calnexin is encoded by the gene CANX.

GroEL is a protein which belongs to the chaperonin family of molecular chaperones, and is found in many bacteria. It is required for the proper folding of many proteins. To function properly, GroEL requires the lid-like cochaperonin protein complex GroES. In eukaryotes the organellar proteins Hsp60 and Hsp10 are structurally and functionally nearly identical to GroEL and GroES, respectively, due to their endosymbiotic origin.

Heat shock 70 kDa protein 8 also known as heat shock cognate 71 kDa protein or Hsc70 or Hsp73 is a heat shock protein that in humans is encoded by the HSPA8 gene on chromosome 11. As a member of the heat shock protein 70 family and a chaperone protein, it facilitates the proper folding of newly translated and misfolded proteins, as well as stabilize or degrade mutant proteins. Its functions contribute to biological processes including signal transduction, apoptosis, autophagy, protein homeostasis, and cell growth and differentiation. It has been associated with an extensive number of cancers,

protein-coding gene in the species Homo sapiens

thumb|Fig 2. Cartoon image of nucleoplasmin core thumb|Fig 3. Comparison of NPM family domains in humans and Xenopus (original diagram in Spanish). Nucleoplasmin (NPM2), the first identified molecular chaperone, is a thermostable acidic protein with a pentameric structure. The protein was first isolated from Xenopus species, and is now recognized as a highly conserved histone chaperone found across animals and other eukaryotes.