1f6w
From Proteopedia
(New page: 200px<br /> <applet load="1f6w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f6w, resolution 2.30Å" /> '''STRUCTURE OF THE CA...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1f6w. | + | [[Image:1f6w.jpg|left|200px]]<br /><applet load="1f6w" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1f6w" size=" | + | |
caption="1f6w, resolution 2.30Å" /> | caption="1f6w, resolution 2.30Å" /> | ||
'''STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT ACTIVATED LIPASE'''<br /> | '''STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT ACTIVATED LIPASE'''<br /> | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1F6W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] Full crystallographic information is available from [http:// | + | 1F6W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F6W OCA]. |
==Reference== | ==Reference== | ||
| Line 24: | Line 23: | ||
[[Category: esterase]] | [[Category: esterase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:46:14 2008'' |
Revision as of 13:46, 15 February 2008
|
STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT ACTIVATED LIPASE
Contents |
Overview
Bile-salt activated lipase (BAL) is a pancreatic enzyme that digests a, variety of lipids in the small intestine. A distinct property of BAL is, its dependency on bile salts in hydrolyzing substrates of long acyl chains, or bulky alcoholic motifs. A crystal structure of the catalytic domain of, human BAL (residues 1-538) with two surface mutations (N186D and A298D), which were introduced in attempting to facilitate crystallization, has, been determined at 2.3 A resolution. The crystal form belongs to space, group P2(1)2(1)2(1) with one monomer per asymmetric unit, and the protein, shows an alpha/beta hydrolase fold. In the absence of bound bile salt, molecules, the protein possesses a preformed catalytic triad and a, functional oxyanion hole. Several surface loops around the active site are, mobile, including two loops potentially involved in substrate binding, (residues 115-125 and 270-285).
Disease
Known disease associated with this structure: Maturity-onset diabetes of the young, type VIII OMIM:[114840]
About this Structure
1F6W is a Single protein structure of sequence from Homo sapiens. Active as Triacylglycerol lipase, with EC number 3.1.1.3 Full crystallographic information is available from OCA.
Reference
Crystal structure of the catalytic domain of human bile salt activated lipase., Terzyan S, Wang CS, Downs D, Hunter B, Zhang XC, Protein Sci. 2000 Sep;9(9):1783-90. PMID:11045623
Page seeded by OCA on Fri Feb 15 15:46:14 2008
