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| - | [[Image:1akn.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1akn| PDB=1akn | SCENE= }} | | {{STRUCTURE_1akn| PDB=1akn | SCENE= }} |
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| - | '''STRUCTURE OF BILE-SALT ACTIVATED LIPASE'''
| + | ===STRUCTURE OF BILE-SALT ACTIVATED LIPASE=== |
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| - | ==Overview==
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| - | BACKGROUND: The intestinally located pancreatic enzyme, bile salt activated lipase (BAL), possesses unique activities for digesting different kinds of lipids. It also differs from other lipases in a requirement of bile salts for activity. A structure-based explanation for these unique properties has not been reached so far due to the absence of a three-dimensional structure. RESULTS: The crystal structures of bovine BAL and its complex with taurocholate have been determined at 2.8 A resolution. The overall structure of BAL belongs to the alpha/beta hydrolase fold family. Two bile salt binding sites were found in each BAL molecule within the BAL-taurocholate complex structure. One of these sites is located close to a hairpin loop near the active site. Upon the binding of taurocholate, this loop becomes less mobile and assumes a different conformation. The other bile salt binding site is located remote from the active site. In both structures, BAL forms similar dimers with the active sites facing each other. CONCLUSIONS: Bile salts activate BAL by binding to a relatively short ten-residue loop near the active site, and stabilize the loop in an open conformation. Presumably, this conformational change leads to the formation of the substrate-binding site, as suggested from kinetic data. The BAL dimer observed in the crystal structure may also play a functional role under physiological conditions.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9331420}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9331420 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9331420}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Serine esterase]] | | [[Category: Serine esterase]] |
| | [[Category: Signal]] | | [[Category: Signal]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:23:26 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:02:49 2008'' |
Revision as of 14:02, 30 June 2008
Template:STRUCTURE 1akn
STRUCTURE OF BILE-SALT ACTIVATED LIPASE
Template:ABSTRACT PUBMED 9331420
About this Structure
1AKN is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
The crystal structure of bovine bile salt activated lipase: insights into the bile salt activation mechanism., Wang X, Wang CS, Tang J, Dyda F, Zhang XC, Structure. 1997 Sep 15;5(9):1209-18. PMID:9331420
Page seeded by OCA on Mon Jun 30 17:02:49 2008
