4l1e: Difference between revisions
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''' | ==Crystal structure of C-Phycocyanin from Leptolyngbya sp. N62DM== | ||
<StructureSection load='4l1e' size='340' side='right' caption='[[4l1e]], [[Resolution|resolution]] 2.61Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4l1e]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Leptolyngbya_sp._n62dm Leptolyngbya sp. n62dm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L1E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L1E FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BLA:BILIVERDINE+IX+ALPHA'>BLA</scene>, <scene name='pdbligand=CYC:PHYCOCYANOBILIN'>CYC</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kvs|3kvs]], [[2uum|2uum]], [[1gh0|1gh0]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4l1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l1e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l1e RCSB], [http://www.ebi.ac.uk/pdbsum/4l1e PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Alzheimer's disease (AD) represents a neurological disorder, which is caused by enzymatic degradation of an amyloid precursor protein into short peptide fragments that undergo association to form insoluble plaques. Preliminary studies suggest that cyanobacterial extracts, especially the light-harvesting protein phycocyanin, may provide a means to control the progression of the disease. However, the molecular mechanism of disease control remains elusive. In the present study, intact hexameric phycocyanin was isolated and crystallized from the cyanobacterium Leptolyngbya sp. N62DM, and the structure was solved to a resolution of 2.6 A. Molecular docking studies show that the phycocyanin alphabeta-dimer interacts with the enzyme beta-secretase, which catalyzes the proteolysis of the amyloid precursor protein to form plaques. The molecular docking studies suggest that the interaction between phycocyanin and beta-secretase is energetically more favorable than previously reported inhibitor-beta-secretase interactions. Transgenic Caenorhabditis elegans worms, with a genotype to serve as an AD-model, were significantly protected by phycocyanin. Therefore, the present study provides a novel structure-based molecular mechanism of phycocyanin-mediated therapy against AD. | |||
Crystal Structure and Interaction of Phycocyanin with beta-Secretase: A Putative Therapy for Alzheimer's Disease.,Singh NK, Hasan SS, Kumar J, Raj I, Pathan AA, Parmar A, Shakil S, Gourinath S, Madamwar D CNS Neurol Disord Drug Targets. 2014 Feb 27. PMID:24576002<ref>PMID:24576002</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Leptolyngbya sp. n62dm]] | |||
[[Category: Gourinath, S.]] | |||
[[Category: Madamwar, D.]] | |||
[[Category: Raj, I.]] | |||
[[Category: Singh, N K.]] | |||
[[Category: Alpha-beta dimer]] | |||
[[Category: Light harvesting protein]] | |||
[[Category: Photosynthesis]] | |||
[[Category: Thylakoid membrane]] | |||
Revision as of 11:57, 21 May 2014
Crystal structure of C-Phycocyanin from Leptolyngbya sp. N62DMCrystal structure of C-Phycocyanin from Leptolyngbya sp. N62DM
Structural highlights
Publication Abstract from PubMedAlzheimer's disease (AD) represents a neurological disorder, which is caused by enzymatic degradation of an amyloid precursor protein into short peptide fragments that undergo association to form insoluble plaques. Preliminary studies suggest that cyanobacterial extracts, especially the light-harvesting protein phycocyanin, may provide a means to control the progression of the disease. However, the molecular mechanism of disease control remains elusive. In the present study, intact hexameric phycocyanin was isolated and crystallized from the cyanobacterium Leptolyngbya sp. N62DM, and the structure was solved to a resolution of 2.6 A. Molecular docking studies show that the phycocyanin alphabeta-dimer interacts with the enzyme beta-secretase, which catalyzes the proteolysis of the amyloid precursor protein to form plaques. The molecular docking studies suggest that the interaction between phycocyanin and beta-secretase is energetically more favorable than previously reported inhibitor-beta-secretase interactions. Transgenic Caenorhabditis elegans worms, with a genotype to serve as an AD-model, were significantly protected by phycocyanin. Therefore, the present study provides a novel structure-based molecular mechanism of phycocyanin-mediated therapy against AD. Crystal Structure and Interaction of Phycocyanin with beta-Secretase: A Putative Therapy for Alzheimer's Disease.,Singh NK, Hasan SS, Kumar J, Raj I, Pathan AA, Parmar A, Shakil S, Gourinath S, Madamwar D CNS Neurol Disord Drug Targets. 2014 Feb 27. PMID:24576002[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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