1n8s
From Proteopedia
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| - | [[Image:1n8s.jpg|left|200px]] | + | [[Image:1n8s.jpg|left|200px]] |
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| - | '''Structure of the pancreatic lipase-colipase complex''' | + | {{Structure |
| + | |PDB= 1n8s |SIZE=350|CAPTION= <scene name='initialview01'>1n8s</scene>, resolution 3.04Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structure of the pancreatic lipase-colipase complex''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1N8S is a [ | + | 1N8S is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N8S OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of the pancreatic lipase-procolipase complex., van Tilbeurgh H, Sarda L, Verger R, Cambillau C, Nature. 1992 Sep 10;359(6391):159-62. PMID:[http:// | + | Structure of the pancreatic lipase-procolipase complex., van Tilbeurgh H, Sarda L, Verger R, Cambillau C, Nature. 1992 Sep 10;359(6391):159-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1522902 1522902] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: Verger, R.]] | [[Category: Verger, R.]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | [[Category: | + | [[Category: pancrea]] |
[[Category: signal]] | [[Category: signal]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:53:37 2008'' |
Revision as of 10:53, 20 March 2008
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| , resolution 3.04Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Triacylglycerol lipase, with EC number 3.1.1.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of the pancreatic lipase-colipase complex
Contents |
Overview
Interfacial adsorption of pancreatic lipase is strongly dependent on the physical chemical properties of the lipid surface. These properties are affected by amphiphiles such as phospholipids and bile salts. In the presence of such amphiphiles, lipase binding to the interface requires a protein cofactor, colipase. We obtained crystals of the pancreatic lipase-procolipase complex and solved the structure at 3.04 A resolution. Here we describe the structure of procolipase, which essentially consists of three 'fingers' and is topologically comparable to snake toxins. The tips of the fingers contain most of the hydrophobic amino acids and presumably form the interfacial binding site. Lipase binding occurs at the opposite side to this site and involves polar interactions. Determination of the three-dimensional structure of pancreatic lipase has revealed the presence of two domains: an amino-terminal domain, at residues 1-336 containing the active site and a carboxy-terminal domain at residues 337-449 (ref. 6). Procolipase binds exclusively to the C-terminal domain of lipase. No conformational change in the lipase molecule is induced by the binding of procolipase.
Disease
Known disease associated with this structure: Pancreatic lipase deficiency OMIM:[246600]
About this Structure
1N8S is a Protein complex structure of sequences from Homo sapiens and Sus scrofa. Full crystallographic information is available from OCA.
Reference
Structure of the pancreatic lipase-procolipase complex., van Tilbeurgh H, Sarda L, Verger R, Cambillau C, Nature. 1992 Sep 10;359(6391):159-62. PMID:1522902
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