Protein Hfq: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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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'>
+<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 ==
-'''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.
+'''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 ==
-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.
+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 ==