Hypoxia-Inducible factor 1 alpha inhibitor

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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='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=''>
== Function ==
== Function ==
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'''Hypoxia-Inducible factor 1 alpha inhibitor'''. (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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'''Hypoxia-Inducible factor 1 alpha inhibitor''' (FIH-1) 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.
== Relevance ==
== Relevance ==
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== Structural highlights ==
== Structural highlights ==
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<scene name='87/875651/Cv/5'>The 3D structure of a complex of SAP with the small molecule ligand AMP</scene> shows the nucleotide phosphate group bridging two Ca+2 ions and forming hydrogen bonds to Asn, Gln and Try residues of SAP <ref>PMID:9217261</ref>.
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<ref>PMID:9217261</ref>.
</StructureSection>
</StructureSection>

Revision as of 07:36, 23 February 2021

Structure of human pentameric SAP (green, grey, pink, yellow, magenta) complex with AMP and Ca+2 ions (green) (PDB code 1lgn)

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3D Structures of Hypoxia-Inducible factor 1 alpha inhibitor

Updated on 23-February-2021

References

  1. ↑ Pepys MB, Rademacher TW, Amatayakul-Chantler S, Williams P, Noble GE, Hutchinson WL, Hawkins PN, Nelson SR, Gallimore JR, Herbert J, et al.. Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure. Proc Natl Acad Sci U S A. 1994 Jun 7;91(12):5602-6. doi: 10.1073/pnas.91.12.5602. PMID:8202534 doi:http://dx.doi.org/10.1073/pnas.91.12.5602
  2. ↑ Richards DB, Cookson LM, Berges AC, Barton SV, Lane T, Ritter JM, Fontana M, Moon JC, Pinzani M, Gillmore JD, Hawkins PN, Pepys MB. Therapeutic Clearance of Amyloid by Antibodies to Serum Amyloid P Component. N Engl J Med. 2015 Sep 17;373(12):1106-14. doi: 10.1056/NEJMoa1504942. Epub 2015 , Jul 15. PMID:26176329 doi:http://dx.doi.org/10.1056/NEJMoa1504942
  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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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