1prh

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(New page: 200px<br /> <applet load="1prh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1prh, resolution 3.5&Aring;" /> '''THE X-RAY CRYSTAL ST...)
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<applet load="1prh" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1prh, resolution 3.5&Aring;" />
'''THE X-RAY CRYSTAL STRUCTURE OF THE MEMBRANE PROTEIN PROSTAGLANDIN H2 SYNTHASE-1'''<br />
'''THE X-RAY CRYSTAL STRUCTURE OF THE MEMBRANE PROTEIN PROSTAGLANDIN H2 SYNTHASE-1'''<br />
==Overview==
==Overview==
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The three-dimensional structure of prostaglandin H2 synthase-1, an, integral membrane protein, has been determined at 3.5 A resolution by, X-ray crystallography. This bifunctional enzyme comprises three, independent folding units: an epidermal growth factor domain, a, membrane-binding motif and an enzymatic domain. Two adjacent but spatially, distinct active sites were found for its haem-dependent peroxidase and, cyclooxygenase activities. The cyclooxygenase active site is created by a, long, hydrophobic channel that is the site of non-steroidal, anti-inflammatory drug binding. The conformation of the membrane-binding, motif strongly suggests that the enzyme integrates into only one leaflet, of the lipid bilayer and is thus a monotopic membrane protein.
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The three-dimensional structure of prostaglandin H2 synthase-1, an integral membrane protein, has been determined at 3.5 A resolution by X-ray crystallography. This bifunctional enzyme comprises three independent folding units: an epidermal growth factor domain, a membrane-binding motif and an enzymatic domain. Two adjacent but spatially distinct active sites were found for its haem-dependent peroxidase and cyclooxygenase activities. The cyclooxygenase active site is created by a long, hydrophobic channel that is the site of non-steroidal anti-inflammatory drug binding. The conformation of the membrane-binding motif strongly suggests that the enzyme integrates into only one leaflet of the lipid bilayer and is thus a monotopic membrane protein.
==About this Structure==
==About this Structure==
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1PRH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. The following page contains interesting information on the relation of 1PRH with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb17_1.html Cyclooxygenase]]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PRH OCA].
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1PRH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. The following page contains interesting information on the relation of 1PRH with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb17_1.html Cyclooxygenase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRH OCA].
==Reference==
==Reference==
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[[Category: Ovis aries]]
[[Category: Ovis aries]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Garavito, R.M.]]
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[[Category: Garavito, R M.]]
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[[Category: Loll, P.J.]]
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[[Category: Loll, P J.]]
[[Category: Picot, D.]]
[[Category: Picot, D.]]
[[Category: HEM]]
[[Category: HEM]]
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[[Category: peroxidase)]]
[[Category: peroxidase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:04:48 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:31:47 2008''

Revision as of 12:31, 21 February 2008


1prh, resolution 3.5Å

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THE X-RAY CRYSTAL STRUCTURE OF THE MEMBRANE PROTEIN PROSTAGLANDIN H2 SYNTHASE-1

Overview

The three-dimensional structure of prostaglandin H2 synthase-1, an integral membrane protein, has been determined at 3.5 A resolution by X-ray crystallography. This bifunctional enzyme comprises three independent folding units: an epidermal growth factor domain, a membrane-binding motif and an enzymatic domain. Two adjacent but spatially distinct active sites were found for its haem-dependent peroxidase and cyclooxygenase activities. The cyclooxygenase active site is created by a long, hydrophobic channel that is the site of non-steroidal anti-inflammatory drug binding. The conformation of the membrane-binding motif strongly suggests that the enzyme integrates into only one leaflet of the lipid bilayer and is thus a monotopic membrane protein.

About this Structure

1PRH is a Single protein structure of sequence from Ovis aries with as ligand. The following page contains interesting information on the relation of 1PRH with [Cyclooxygenase]. Full crystallographic information is available from OCA.

Reference

The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1., Picot D, Loll PJ, Garavito RM, Nature. 1994 Jan 20;367(6460):243-9. PMID:8121489

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