1ddx

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(New page: 200px<br /><applet load="1ddx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ddx, resolution 3.00&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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'''CRYSTAL STRUCTURE OF A MIXTURE OF ARACHIDONIC ACID AND PROSTAGLANDIN BOUND TO THE CYCLOOXYGENASE ACTIVE SITE OF COX-2: PROSTAGLANDIN STRUCTURE'''<br />
'''CRYSTAL STRUCTURE OF A MIXTURE OF ARACHIDONIC ACID AND PROSTAGLANDIN BOUND TO THE CYCLOOXYGENASE ACTIVE SITE OF COX-2: PROSTAGLANDIN STRUCTURE'''<br />
==Overview==
==Overview==
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Cyclooxygenases are bifunctional enzymes that catalyse the first committed, step in the synthesis of prostaglandins, thromboxanes and other, eicosanoids. The two known cyclooxygenases isoforms share a high degree of, amino-acid sequence similarity, structural topology and an identical, catalytic mechanism. Cyclooxygenase enzymes catalyse two sequential, reactions in spatially distinct, but mechanistically coupled active sites., The initial cyclooxygenase reaction converts arachidonic acid (which is, achiral) to prostaglandin G2 (which has five chiral centres). The, subsequent peroxidase reaction reduces prostaglandin G2 to prostaglandin, H2. Here we report the co-crystal structures of murine, apo-cyclooxygenase-2 in complex with arachidonic acid and prostaglandin., These structures suggest the molecular basis for the stereospecificity of, prostaglandin G2 synthesis.
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Cyclooxygenases are bifunctional enzymes that catalyse the first committed step in the synthesis of prostaglandins, thromboxanes and other eicosanoids. The two known cyclooxygenases isoforms share a high degree of amino-acid sequence similarity, structural topology and an identical catalytic mechanism. Cyclooxygenase enzymes catalyse two sequential reactions in spatially distinct, but mechanistically coupled active sites. The initial cyclooxygenase reaction converts arachidonic acid (which is achiral) to prostaglandin G2 (which has five chiral centres). The subsequent peroxidase reaction reduces prostaglandin G2 to prostaglandin H2. Here we report the co-crystal structures of murine apo-cyclooxygenase-2 in complex with arachidonic acid and prostaglandin. These structures suggest the molecular basis for the stereospecificity of prostaglandin G2 synthesis.
==About this Structure==
==About this Structure==
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1DDX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NAG, BOG and PGX as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Prostaglandin-endoperoxide_synthase Prostaglandin-endoperoxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.1 1.14.99.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DDX OCA].
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1DDX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=BOG:'>BOG</scene> and <scene name='pdbligand=PGX:'>PGX</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Prostaglandin-endoperoxide_synthase Prostaglandin-endoperoxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.1 1.14.99.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DDX OCA].
==Reference==
==Reference==
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[[Category: Prostaglandin-endoperoxide synthase]]
[[Category: Prostaglandin-endoperoxide synthase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Gierse, J.K.]]
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[[Category: Gierse, J K.]]
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[[Category: Goodwin, D.C.]]
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[[Category: Goodwin, D C.]]
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[[Category: Kiefer, J.R.]]
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[[Category: Kiefer, J R.]]
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[[Category: Kurumbail, R.G.]]
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[[Category: Kurumbail, R G.]]
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[[Category: Marnett, L.J.]]
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[[Category: Marnett, L J.]]
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[[Category: Moreland, K.T.]]
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[[Category: Moreland, K T.]]
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[[Category: Pawlitz, J.L.]]
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[[Category: Pawlitz, J L.]]
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[[Category: Rowlinson, S.W.]]
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[[Category: Rowlinson, S W.]]
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[[Category: Stallings, W.C.]]
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[[Category: Stallings, W C.]]
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[[Category: Stegeman, R.A.]]
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[[Category: Stegeman, R A.]]
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[[Category: Stevens, A.M.]]
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[[Category: Stevens, A M.]]
[[Category: BOG]]
[[Category: BOG]]
[[Category: NAG]]
[[Category: NAG]]
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[[Category: prostaglandin]]
[[Category: prostaglandin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:12:13 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:37 2008''

Revision as of 10:15, 21 February 2008


1ddx, resolution 3.00Å

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CRYSTAL STRUCTURE OF A MIXTURE OF ARACHIDONIC ACID AND PROSTAGLANDIN BOUND TO THE CYCLOOXYGENASE ACTIVE SITE OF COX-2: PROSTAGLANDIN STRUCTURE

Overview

Cyclooxygenases are bifunctional enzymes that catalyse the first committed step in the synthesis of prostaglandins, thromboxanes and other eicosanoids. The two known cyclooxygenases isoforms share a high degree of amino-acid sequence similarity, structural topology and an identical catalytic mechanism. Cyclooxygenase enzymes catalyse two sequential reactions in spatially distinct, but mechanistically coupled active sites. The initial cyclooxygenase reaction converts arachidonic acid (which is achiral) to prostaglandin G2 (which has five chiral centres). The subsequent peroxidase reaction reduces prostaglandin G2 to prostaglandin H2. Here we report the co-crystal structures of murine apo-cyclooxygenase-2 in complex with arachidonic acid and prostaglandin. These structures suggest the molecular basis for the stereospecificity of prostaglandin G2 synthesis.

About this Structure

1DDX is a Single protein structure of sequence from Mus musculus with , and as ligands. Active as Prostaglandin-endoperoxide synthase, with EC number 1.14.99.1 Full crystallographic information is available from OCA.

Reference

Structural insights into the stereochemistry of the cyclooxygenase reaction., Kiefer JR, Pawlitz JL, Moreland KT, Stegeman RA, Hood WF, Gierse JK, Stevens AM, Goodwin DC, Rowlinson SW, Marnett LJ, Stallings WC, Kurumbail RG, Nature. 2000 May 4;405(6782):97-101. PMID:10811226

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