From Wikipedia, the free encyclopedia
BRICHOS domain
Human SP-C BRICHOS domain, extracted monomer ( PDB: 2yad​)
Identifiers
SymbolBRICHOS
Pfam PF04089
InterPro IPR007084
PROSITE PDOC50869
CATH 2yadA00
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

The BRICHOS family consists of a variety of proteins linked to major diseases, each containing a 100 amino acid BRICHOS domain that is thought to have a chaperone function. [1] [2] These include BRI2, which is related to familial British and Danish dementia (FBD and FDD); Chondromodulin-I, related to chondrosarcoma; CA11, related to stomach cancer; and surfactant protein C (SP-C), related to respiratory distress syndrome (RDS).

Further reading

  • Johansson H, Eriksson M, Nordling K, Presto J, Johansson J (June 2009). "The Brichos domain of prosurfactant protein C can hold and fold a transmembrane segment". Protein Sci. 18 (6): 1175–82. doi: 10.1002/pro.123. PMC  2774428. PMID  19472327.
  • Johansson H, Nordling K, Weaver TE, Johansson J (July 2006). "The Brichos domain-containing C-terminal part of pro-surfactant protein C binds to an unfolded poly-val transmembrane segment". J. Biol. Chem. 281 (30): 21032–9. doi: 10.1074/jbc.M603001200. PMID  16709565.
  • Mulugeta S, Nguyen V, Russo SJ, Muniswamy M, Beers MF (June 2005). "A surfactant protein C precursor protein BRICHOS domain mutation causes endoplasmic reticulum stress, proteasome dysfunction, and caspase 3 activation". Am. J. Respir. Cell Mol. Biol. 32 (6): 521–30. doi: 10.1165/rcmb.2005-0009OC. PMC  2715321. PMID  15778495.

References

  1. ^ Sánchez-Pulido L, Devos D, Valencia A (July 2002). "BRICHOS: a conserved domain in proteins associated with dementia, respiratory distress and cancer". Trends Biochem. Sci. 27 (7): 329–32. doi: 10.1016/s0968-0004(02)02134-5. PMID  12114016.
  2. ^ Hedlund J, Johansson J, Persson B (2009). "BRICHOS - a superfamily of multidomain proteins with diverse functions". BMC Res Notes. 2: 180. doi: 10.1186/1756-0500-2-180. PMC  2751770. PMID  19747390.
From Wikipedia, the free encyclopedia
BRICHOS domain
Human SP-C BRICHOS domain, extracted monomer ( PDB: 2yad​)
Identifiers
SymbolBRICHOS
Pfam PF04089
InterPro IPR007084
PROSITE PDOC50869
CATH 2yadA00
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

The BRICHOS family consists of a variety of proteins linked to major diseases, each containing a 100 amino acid BRICHOS domain that is thought to have a chaperone function. [1] [2] These include BRI2, which is related to familial British and Danish dementia (FBD and FDD); Chondromodulin-I, related to chondrosarcoma; CA11, related to stomach cancer; and surfactant protein C (SP-C), related to respiratory distress syndrome (RDS).

Further reading

  • Johansson H, Eriksson M, Nordling K, Presto J, Johansson J (June 2009). "The Brichos domain of prosurfactant protein C can hold and fold a transmembrane segment". Protein Sci. 18 (6): 1175–82. doi: 10.1002/pro.123. PMC  2774428. PMID  19472327.
  • Johansson H, Nordling K, Weaver TE, Johansson J (July 2006). "The Brichos domain-containing C-terminal part of pro-surfactant protein C binds to an unfolded poly-val transmembrane segment". J. Biol. Chem. 281 (30): 21032–9. doi: 10.1074/jbc.M603001200. PMID  16709565.
  • Mulugeta S, Nguyen V, Russo SJ, Muniswamy M, Beers MF (June 2005). "A surfactant protein C precursor protein BRICHOS domain mutation causes endoplasmic reticulum stress, proteasome dysfunction, and caspase 3 activation". Am. J. Respir. Cell Mol. Biol. 32 (6): 521–30. doi: 10.1165/rcmb.2005-0009OC. PMC  2715321. PMID  15778495.

References

  1. ^ Sánchez-Pulido L, Devos D, Valencia A (July 2002). "BRICHOS: a conserved domain in proteins associated with dementia, respiratory distress and cancer". Trends Biochem. Sci. 27 (7): 329–32. doi: 10.1016/s0968-0004(02)02134-5. PMID  12114016.
  2. ^ Hedlund J, Johansson J, Persson B (2009). "BRICHOS - a superfamily of multidomain proteins with diverse functions". BMC Res Notes. 2: 180. doi: 10.1186/1756-0500-2-180. PMC  2751770. PMID  19747390.

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