4pf9: Difference between revisions

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'''Unreleased structure'''
==Crystal structure of insulin degrading enzyme complexed with inhibitor==
 
<StructureSection load='4pf9' size='340' side='right' caption='[[4pf9]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
The entry 4pf9 is ON HOLD  until Paper Publication
== Structural highlights ==
 
<table><tr><td colspan='2'>[[4pf9]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PF9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PF9 FirstGlance]. <br>
Authors: Wang, Y., Guo, S.
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2Q6:METHYL+[(2S)-2-[4-({5-[4-({(2S)-2-[(3S)-3-AMINO-2-OXOPIPERIDIN-1-YL]-2-CYCLOHEXYLACETYL}AMINO)PHENYL]PENTYL}OXY)PHENYL]-3-(QUINOLIN-3-YL)PROPYL]CARBAMATE'>2Q6</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pes|4pes]], [[4pf7|4pf7]]</td></tr>
Description:  
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Insulysin Insulysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.56 3.4.24.56] </span></td></tr>
[[Category: Unreleased Structures]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pf9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pf9 RCSB], [http://www.ebi.ac.uk/pdbsum/4pf9 PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/IDE_HUMAN IDE_HUMAN]] Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia.<ref>PMID:10684867</ref> <ref>PMID:17613531</ref> <ref>PMID:18986166</ref> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Insulysin]]
[[Category: Guo, S]]
[[Category: Guo, S]]
[[Category: Wang, Y]]
[[Category: Wang, Y]]
[[Category: Hydrolase-hydrolase inhibitor complex]]

Revision as of 18:20, 17 June 2015

Crystal structure of insulin degrading enzyme complexed with inhibitorCrystal structure of insulin degrading enzyme complexed with inhibitor

Structural highlights

4pf9 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Activity:Insulysin, with EC number 3.4.24.56
Resources:FirstGlance, OCA, RCSB, PDBsum

Function

[IDE_HUMAN] Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia.[1] [2] [3]

References

  1. Vekrellis K, Ye Z, Qiu WQ, Walsh D, Hartley D, Chesneau V, Rosner MR, Selkoe DJ. Neurons regulate extracellular levels of amyloid beta-protein via proteolysis by insulin-degrading enzyme. J Neurosci. 2000 Mar 1;20(5):1657-65. PMID:10684867
  2. Im H, Manolopoulou M, Malito E, Shen Y, Zhao J, Neant-Fery M, Sun CY, Meredith SC, Sisodia SS, Leissring MA, Tang WJ. Structure of substrate-free human insulin-degrading enzyme (IDE) and biophysical analysis of ATP-induced conformational switch of IDE. J Biol Chem. 2007 Aug 31;282(35):25453-63. Epub 2007 Jul 5. PMID:17613531 doi:10.1074/jbc.M701590200
  3. Malito E, Ralat LA, Manolopoulou M, Tsay JL, Wadlington NL, Tang WJ. Molecular Bases for the Recognition of Short Peptide Substrates and Cysteine-Directed Modifications of Human Insulin-Degrading Enzyme. Biochemistry. 2008 Nov 6. PMID:18986166 doi:10.1021/bi801192h

4pf9, resolution 2.50Å

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