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1cjy
From Proteopedia
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| - | [[Image:1cjy.gif|left|200px]] | + | [[Image:1cjy.gif|left|200px]] |
| - | + | ||
| - | '''HUMAN CYTOSOLIC PHOSPHOLIPASE A2''' | + | {{Structure |
| + | |PDB= 1cjy |SIZE=350|CAPTION= <scene name='initialview01'>1cjy</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC ACID'>MES</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HUMAN CYTOSOLIC PHOSPHOLIPASE A2''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CJY is a [ | + | 1CJY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CJY OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of human cytosolic phospholipase A2 reveals a novel topology and catalytic mechanism., Dessen A, Tang J, Schmidt H, Stahl M, Clark JD, Seehra J, Somers WS, Cell. 1999 Apr 30;97(3):349-60. PMID:[http:// | + | Crystal structure of human cytosolic phospholipase A2 reveals a novel topology and catalytic mechanism., Dessen A, Tang J, Schmidt H, Stahl M, Clark JD, Seehra J, Somers WS, Cell. 1999 Apr 30;97(3):349-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10319815 10319815] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Phospholipase A(2)]] | [[Category: Phospholipase A(2)]] | ||
| Line 27: | Line 36: | ||
[[Category: phospholipase]] | [[Category: phospholipase]] | ||
| - | ''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 10:25:19 2008'' |
Revision as of 08:25, 20 March 2008
| |||||||
| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Phospholipase A(2), with EC number 3.1.1.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN CYTOSOLIC PHOSPHOLIPASE A2
Overview
Cytosolic phospholipase A2 initiates the biosynthesis of prostaglandins, leukotrienes, and platelet-activating factor (PAF), mediators of the pathophysiology of asthma and arthritis. Here, we report the X-ray crystal structure of human cPLA2 at 2.5 A. cPLA2 consists of an N-terminal calcium-dependent lipid-binding/C2 domain and a catalytic unit whose topology is distinct from that of other lipases. An unusual Ser-Asp dyad located in a deep cleft at the center of a predominantly hydrophobic funnel selectively cleaves arachidonyl phospholipids. The structure reveals a flexible lid that must move to allow substrate access to the active site, thus explaining the interfacial activation of this important lipase.
About this Structure
1CJY is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of human cytosolic phospholipase A2 reveals a novel topology and catalytic mechanism., Dessen A, Tang J, Schmidt H, Stahl M, Clark JD, Seehra J, Somers WS, Cell. 1999 Apr 30;97(3):349-60. PMID:10319815
Page seeded by OCA on Thu Mar 20 10:25:19 2008
Categories: Homo sapiens | Phospholipase A(2) | Single protein | Clark, J D. | Dessen, A. | Schmidt, H. | Seehra, J. | Somers, W S. | Stahl, M. | Tang, J. | CA | MES | Hydrolase | Lipid-binding | Phospholipase
