1cjy

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(New page: 200px<br /> <applet load="1cjy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cjy, resolution 2.5&Aring;" /> '''HUMAN CYTOSOLIC PHOS...)
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<applet load="1cjy" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1cjy, resolution 2.5&Aring;" />
'''HUMAN CYTOSOLIC PHOSPHOLIPASE A2'''<br />
'''HUMAN CYTOSOLIC PHOSPHOLIPASE A2'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1CJY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA and MES as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CJY OCA].
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1CJY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=MES:'>MES</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CJY OCA].
==Reference==
==Reference==
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[[Category: Phospholipase A(2)]]
[[Category: Phospholipase A(2)]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Clark, J.D.]]
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[[Category: Clark, J D.]]
[[Category: Dessen, A.]]
[[Category: Dessen, A.]]
[[Category: Schmidt, H.]]
[[Category: Schmidt, H.]]
[[Category: Seehra, J.]]
[[Category: Seehra, J.]]
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[[Category: Somers, W.S.]]
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[[Category: Somers, W S.]]
[[Category: Stahl, M.]]
[[Category: Stahl, M.]]
[[Category: Tang, J.]]
[[Category: Tang, J.]]
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[[Category: phospholipase]]
[[Category: phospholipase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:22:33 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:50 2008''

Revision as of 10:06, 21 February 2008


1cjy, resolution 2.5Å

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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 with and as ligands. Active as Phospholipase A(2), with EC number 3.1.1.4 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

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