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Protein Hfq

From Proteopedia

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(New page: <StructureSection load='1lgn' size='340' side='right' caption='Structure of human pentameric SAP (green, grey, pink, yellow, magenta) complex with AMP and Ca+2 ions (green) (PDB code [[1l...)
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<StructureSection load='1lgn' size='340' side='right' caption='Structure of human pentameric SAP (green, grey, pink, yellow, magenta) complex with AMP and Ca+2 ions (green) (PDB code [[1lgn]])' scene='87/875651/Cv/1'>
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<StructureSection load='4ht9' size='340' side='right' caption='Structure of human pentameric SAP (green, grey, pink, yellow, magenta) complex with AMP and Ca+2 ions (green) (PDB code [[4ht9]])' scene='87/875651/Cv/1'>
== Function ==
== Function ==
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'''Serum amyloid P-component''' (SAP) is a plasma protein and is the precursor of amyloid P-component which is constituent of deposits in amyloidosis and Alzheimer disease<ref>PMID:8202534</ref>. SAP binds in a calcium-dependent fashion to a variety of ligands.
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'''Protein Hfq''' (Hfq) ('''H'''ost '''F'''actor for '''Q'''β) or '''RNA-binding protein Hfq''' is stimulating base-pairing between sRNA and target mRNA by binding both RNAs via three RNA-binding surfaces. Hfq is found in enteric bacteria<ref>PMID:30487269</ref>. SAP binds in a calcium-dependent fashion to a variety of ligands.
== Relevance ==
== Relevance ==
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Mutations in SAP affect the aggregation of mutated lysozyme which cause amyloidosis. The inhibition of SAP binding to amyloid fibrils is a therapeutic target in some serious human diseases<ref>PMID:26176329</ref>. Small molecule ligands can displace SAP from amyloid fibrils and can provide therapeutic treatment of amyloidosis.
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Since Hfq is required for gene regulation and infectivity of some Gram-negative bacteria its mutations can eliminate infectivity of Lyme disease caused by the bacteria ''Borellia burgdorferi,'' for example<ref>PMID:20815822</ref>.
== Structural highlights ==
== Structural highlights ==

Revision as of 07:58, 22 February 2021

Structure of human pentameric SAP (green, grey, pink, yellow, magenta) complex with AMP and Ca+2 ions (green) (PDB code 4ht9)

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3D Structures of protein Hfq

Updated on 22-February-2021


References

  1. ↑ Morita T, Aiba H. Mechanism and physiological significance of autoregulation of the Escherichia coli hfq gene. RNA. 2019 Feb;25(2):264-276. doi: 10.1261/rna.068106.118. Epub 2018 Nov 28. PMID:30487269 doi:http://dx.doi.org/10.1261/rna.068106.118
  2. ↑ Lybecker MC, Abel CA, Feig AL, Samuels DS. Identification and function of the RNA chaperone Hfq in the Lyme disease spirochete Borrelia burgdorferi. Mol Microbiol. 2010 Nov;78(3):622-35. doi: 10.1111/j.1365-2958.2010.07374.x. Epub, 2010 Sep 27. PMID:20815822 doi:http://dx.doi.org/10.1111/j.1365-2958.2010.07374.x
  3. ↑ Hohenester E, Hutchinson WL, Pepys MB, Wood SP. Crystal structure of a decameric complex of human serum amyloid P component with bound dAMP. J Mol Biol. 1997 Jun 20;269(4):570-8. PMID:9217261 doi:10.1006/jmbi.1997.1075

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