1rlw

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[[Image:1rlw.gif|left|200px]]<br /><applet load="1rlw" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1rlw.gif|left|200px]]
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caption="1rlw, resolution 2.4&Aring;" />
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'''CALCIUM-PHOSPHOLIPID BINDING DOMAIN FROM CYTOSOLIC PHOSPHOLIPASE A2'''<br />
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{{Structure
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|PDB= 1rlw |SIZE=350|CAPTION= <scene name='initialview01'>1rlw</scene>, resolution 2.4&Aring;
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|SITE= <scene name='pdbsite=CA1:Ca+Site+I'>CA1</scene>, <scene name='pdbsite=CA2:Ca+Site+II'>CA2</scene>, <scene name='pdbsite=CR1:Ca-Binding+Region+1'>CR1</scene>, <scene name='pdbsite=CR2:Ca-Binding+Region+2'>CR2</scene> and <scene name='pdbsite=CR3:Ca-Binding+Region+3'>CR3</scene>
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|LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|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]
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|GENE=
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}}
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'''CALCIUM-PHOSPHOLIPID BINDING DOMAIN FROM CYTOSOLIC PHOSPHOLIPASE A2'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1RLW 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=CD:'>CD</scene> and <scene name='pdbligand=CA:'>CA</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] Known structural/functional Sites: <scene name='pdbsite=CA1:Ca+Site+I'>CA1</scene>, <scene name='pdbsite=CA2:Ca+Site+II'>CA2</scene>, <scene name='pdbsite=CR1:Ca-Binding+Region+1'>CR1</scene>, <scene name='pdbsite=CR2:Ca-Binding+Region+2'>CR2</scene> and <scene name='pdbsite=CR3:Ca-Binding+Region+3'>CR3</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RLW OCA].
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1RLW 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=1RLW OCA].
==Reference==
==Reference==
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Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2., Perisic O, Fong S, Lynch DE, Bycroft M, Williams RL, J Biol Chem. 1998 Jan 16;273(3):1596-604. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9430701 9430701]
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Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2., Perisic O, Fong S, Lynch DE, Bycroft M, Williams RL, J Biol Chem. 1998 Jan 16;273(3):1596-604. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9430701 9430701]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Phospholipase A(2)]]
[[Category: Phospholipase A(2)]]
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[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:52:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:53:22 2008''

Revision as of 11:53, 20 March 2008

Image:1rlw.gif


PDB ID 1rlw

Drag the structure with the mouse to rotate
, resolution 2.4Å
Sites: , , , and
Ligands: and
Activity: Phospholipase A(2), with EC number 3.1.1.4
Coordinates: save as pdb, mmCIF, xml



CALCIUM-PHOSPHOLIPID BINDING DOMAIN FROM CYTOSOLIC PHOSPHOLIPASE A2


Overview

Cytosolic phospholipase A2 (cPLA2) is a calcium-sensitive 85-kDa enzyme that hydrolyzes arachidonic acid-containing membrane phospholipids to initiate the biosynthesis of eicosanoids and platelet-activating factor, potent inflammatory mediators. The calcium-dependent activation of the enzyme is mediated by an N-terminal C2 domain, which is responsible for calcium-dependent translocation of the enzyme to membranes and that enables the intact enzyme to hydrolyze membrane-resident substrates. The 2.4-A x-ray crystal structure of this C2 domain was solved by multiple isomorphous replacement and reveals a beta-sandwich with the same topology as the C2 domain from phosphoinositide-specific phospholipase C delta 1. Two clusters of exposed hydrophobic residues surround two adjacent calcium binding sites. This region, along with an adjoining strip of basic residues, appear to constitute the membrane binding motif. The structure provides a striking insight into the relative importance of hydrophobic and electrostatic components of membrane binding for cPLA2. Although hydrophobic interactions predominate for cPLA2, for other C2 domains such as in "conventional" protein kinase C and synaptotagmins, electrostatic forces prevail.

About this Structure

1RLW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2., Perisic O, Fong S, Lynch DE, Bycroft M, Williams RL, J Biol Chem. 1998 Jan 16;273(3):1596-604. PMID:9430701

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