2fyl

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m (Protected "2fyl" [edit=sysop:move=sysop])
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[[Image:2fyl.png|left|200px]]
 
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{{STRUCTURE_2fyl| PDB=2fyl | SCENE= }}
{{STRUCTURE_2fyl| PDB=2fyl | SCENE= }}
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===Haddock model of the complex between double module of LRP, CR56, and first domain of receptor associated protein, RAP-d1.===
===Haddock model of the complex between double module of LRP, CR56, and first domain of receptor associated protein, RAP-d1.===
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{{ABSTRACT_PUBMED_16938309}}
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{{ABSTRACT_PUBMED_16938309}}
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==Disease==
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[[http://www.uniprot.org/uniprot/AMRP_HUMAN AMRP_HUMAN]] Note=In complex with the alpha-2-MR or gp330, it may have some role in the pathogenesis of membrane glomerular nephritis.
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==Function==
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[[http://www.uniprot.org/uniprot/AMRP_HUMAN AMRP_HUMAN]] Interacts with LRP1/alpha-2-macroglobulin receptor and glycoprotein 330. [[http://www.uniprot.org/uniprot/LRP1_HUMAN LRP1_HUMAN]] Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells. Required for early embryonic development. Involved in cellular lipid homeostasis. Involved in the plasma clearance of chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as the local metabolism of complexes between plasminogen activators and their endogenous inhibitors. May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission.<ref>PMID:1702392</ref><ref>PMID:1618748</ref><ref>PMID:11907044</ref><ref>PMID:12888553</ref><ref>PMID:12713657</ref> Functions as a receptor for Pseudomonas aeruginosa exotoxin A.<ref>PMID:1702392</ref><ref>PMID:1618748</ref><ref>PMID:11907044</ref><ref>PMID:12888553</ref><ref>PMID:12713657</ref>
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:016938309</ref><references group="xtra"/>
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<ref group="xtra">PMID:016938309</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Andersen, O M.]]
[[Category: Andersen, O M.]]

Revision as of 11:49, 24 March 2013

Template:STRUCTURE 2fyl

Contents

Haddock model of the complex between double module of LRP, CR56, and first domain of receptor associated protein, RAP-d1.

Template:ABSTRACT PUBMED 16938309

Disease

[AMRP_HUMAN] Note=In complex with the alpha-2-MR or gp330, it may have some role in the pathogenesis of membrane glomerular nephritis.

Function

[AMRP_HUMAN] Interacts with LRP1/alpha-2-macroglobulin receptor and glycoprotein 330. [LRP1_HUMAN] Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells. Required for early embryonic development. Involved in cellular lipid homeostasis. Involved in the plasma clearance of chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as the local metabolism of complexes between plasminogen activators and their endogenous inhibitors. May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission.[1][2][3][4][5] Functions as a receptor for Pseudomonas aeruginosa exotoxin A.[6][7][8][9][10]

About this Structure

2fyl is a 2 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

  • Jensen GA, Andersen OM, Bonvin AM, Bjerrum-Bohr I, Etzerodt M, Thogersen HC, O'Shea C, Poulsen FM, Kragelund BB. Binding site structure of one LRP-RAP complex: implications for a common ligand-receptor binding motif. J Mol Biol. 2006 Sep 29;362(4):700-16. Epub 2006 Jul 15. PMID:16938309 doi:10.1016/j.jmb.2006.07.013
  1. ↑ Kristensen T, Moestrup SK, Gliemann J, Bendtsen L, Sand O, Sottrup-Jensen L. Evidence that the newly cloned low-density-lipoprotein receptor related protein (LRP) is the alpha 2-macroglobulin receptor. FEBS Lett. 1990 Dec 10;276(1-2):151-5. PMID:1702392
  2. ↑ Kounnas MZ, Morris RE, Thompson MR, FitzGerald DJ, Strickland DK, Saelinger CB. The alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein binds and internalizes Pseudomonas exotoxin A. J Biol Chem. 1992 Jun 25;267(18):12420-3. PMID:1618748
  3. ↑ May P, Reddy YK, Herz J. Proteolytic processing of low density lipoprotein receptor-related protein mediates regulated release of its intracellular domain. J Biol Chem. 2002 May 24;277(21):18736-43. Epub 2002 Mar 20. PMID:11907044 doi:10.1074/jbc.M201979200
  4. ↑ Kinoshita A, Shah T, Tangredi MM, Strickland DK, Hyman BT. The intracellular domain of the low density lipoprotein receptor-related protein modulates transactivation mediated by amyloid precursor protein and Fe65. J Biol Chem. 2003 Oct 17;278(42):41182-8. Epub 2003 Jul 29. PMID:12888553 doi:10.1074/jbc.M306403200
  5. ↑ May P, Herz J. LDL receptor-related proteins in neurodevelopment. Traffic. 2003 May;4(5):291-301. PMID:12713657
  6. ↑ Kristensen T, Moestrup SK, Gliemann J, Bendtsen L, Sand O, Sottrup-Jensen L. Evidence that the newly cloned low-density-lipoprotein receptor related protein (LRP) is the alpha 2-macroglobulin receptor. FEBS Lett. 1990 Dec 10;276(1-2):151-5. PMID:1702392
  7. ↑ Kounnas MZ, Morris RE, Thompson MR, FitzGerald DJ, Strickland DK, Saelinger CB. The alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein binds and internalizes Pseudomonas exotoxin A. J Biol Chem. 1992 Jun 25;267(18):12420-3. PMID:1618748
  8. ↑ May P, Reddy YK, Herz J. Proteolytic processing of low density lipoprotein receptor-related protein mediates regulated release of its intracellular domain. J Biol Chem. 2002 May 24;277(21):18736-43. Epub 2002 Mar 20. PMID:11907044 doi:10.1074/jbc.M201979200
  9. ↑ Kinoshita A, Shah T, Tangredi MM, Strickland DK, Hyman BT. The intracellular domain of the low density lipoprotein receptor-related protein modulates transactivation mediated by amyloid precursor protein and Fe65. J Biol Chem. 2003 Oct 17;278(42):41182-8. Epub 2003 Jul 29. PMID:12888553 doi:10.1074/jbc.M306403200
  10. ↑ May P, Herz J. LDL receptor-related proteins in neurodevelopment. Traffic. 2003 May;4(5):291-301. PMID:12713657

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