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| - | [[Image:2b00.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2b00| PDB=2b00 | SCENE= }} | | {{STRUCTURE_2b00| PDB=2b00 | SCENE= }} |
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| - | '''Crystal Structure of Porcine Pancreatic Phospholipase A2 in Complex with Glycocholate'''
| + | ===Crystal Structure of Porcine Pancreatic Phospholipase A2 in Complex with Glycocholate=== |
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| - | ==Overview==
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| - | Bile salt interactions with phospholipid monolayers of fat emulsions are known to regulate the actions of gastrointestinal lipolytic enzymes in order to control the uptake of dietary fat. Specifically, on the lipid/aqueous interface of fat emulsions, the anionic portions of amphipathic bile salts have been thought to interact with and activate the enzyme group-IB phospholipase A2 (PLA2) derived from the pancreas. To explore this regulatory process, we have determined the crystal structures of the complexes of pancreatic PLA2 with the naturally occurring bile salts: cholate, glycocholate, taurocholate, glycochenodeoxycholate, and taurochenodeoxycholate. The five PLA2-bile salt complexes each result in a partly occluded active site, and the resulting ligand binding displays specific hydrogen bonding interactions and extensive hydrophobic packing. The amphipathic bile salts are bound to PLA2 with their polar hydroxyl and sulfate/carboxy groups oriented away from the enzyme's hydrophobic core. The impaired catalytic and interface binding functions implied by these structures provide a basis for the previous numerous observations of a biphasic dependence of the rate of PLA2 catalyzed hydrolysis of zwitterionic glycerophospholipids in the presence of bile salts. The rising or activation phase is consistent with enhanced binding and activation of the bound PLA2 by the bile salt induced anionic charge in a zwitterionic interface. The falling or inhibitory phase can be explained by the formation of a catalytically inert stoichiometric complex between PLA2 and any bile salts in which it forms a stable complex. The model provides new insight into the regulatory role that specific PLA2-bile salt interactions are likely to play in fat metabolism.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17434532}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17434532 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17434532}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Pancreatic enzyme]] | | [[Category: Pancreatic enzyme]] |
| | [[Category: Pla2]] | | [[Category: Pla2]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:40:56 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:47:49 2008'' |
Revision as of 12:47, 28 July 2008
Template:STRUCTURE 2b00
Crystal Structure of Porcine Pancreatic Phospholipase A2 in Complex with Glycocholate
Template:ABSTRACT PUBMED 17434532
About this Structure
2B00 is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
Structural basis for bile salt inhibition of pancreatic phospholipase A2., Pan YH, Bahnson BJ, J Mol Biol. 2007 Jun 1;369(2):439-50. Epub 2007 Mar 20. PMID:17434532
Page seeded by OCA on Mon Jul 28 15:47:49 2008
