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1f6w

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Revision as of 09:23, 27 December 2017

STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT ACTIVATED LIPASE

Structural highlights

1f6w is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1akn
Activity:	Triacylglycerol lipase, with EC number 3.1.1.3
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[CEL_HUMAN] Defects in CEL are a cause of maturity-onset diabetes of the young type 8 with exocrine dysfunction (MODY8) [MIM:609812]; also known as diabetes and pancreatic exocrine dysfunction (DPED). MODY is a form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease.^[1]

Function

[CEL_HUMAN] Catalyzes fat and vitamin absorption. Acts in concert with pancreatic lipase and colipase for the complete digestion of dietary triglycerides.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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).

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Raeder H, Johansson S, Holm PI, Haldorsen IS, Mas E, Sbarra V, Nermoen I, Eide SA, Grevle L, Bjorkhaug L, Sagen JV, Aksnes L, Sovik O, Lombardo D, Molven A, Njolstad PR. Mutations in the CEL VNTR cause a syndrome of diabetes and pancreatic exocrine dysfunction. Nat Genet. 2006 Jan;38(1):54-62. Epub 2005 Dec 20. PMID:16369531 doi:10.1038/ng1708
↑ Terzyan S, Wang CS, Downs D, Hunter B, Zhang XC. Crystal structure of the catalytic domain of human bile salt activated lipase. Protein Sci. 2000 Sep;9(9):1783-90. PMID:11045623

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1f6w"

@@ Line 1: / Line 1: @@
 ==STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT ACTIVATED LIPASE==
 <StructureSection load='1f6w' size='340' side='right' caption='[[1f6w]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1akn|1akn]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
-<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=1f6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f6w OCA], [http://pdbe.org/1f6w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f6w RCSB], [http://www.ebi.ac.uk/pdbsum/1f6w PDBsum]</span></td></tr>
+<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=1f6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f6w OCA], [http://pdbe.org/1f6w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f6w RCSB], [http://www.ebi.ac.uk/pdbsum/1f6w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1f6w ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 15: / Line 16: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f6/1f6w_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f6/1f6w_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 30: / Line 31: @@
 </div>
 <div class="pdbe-citations 1f6w" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Cholesterol esterase|Cholesterol esterase]]
-*[[Lipase|Lipase]]
 == References ==
 <references/>

1f6w

From Proteopedia

Revision as of 09:23, 27 December 2017

STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT ACTIVATED LIPASE

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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