3hfb - Revision history

OCA at 09:59, 21 February 2024

OCA — Wed, 21 Feb 2024 09:59:35 GMT

←Older revision		Revision as of 09:59, 21 February 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3hfb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HFB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HFB FirstGlance]. <br>		<table><tr><td colspan='2'>[[3hfb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HFB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HFB FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>~~, ~~<scene name='pdbligand=ML4:4-(5-{~~[~~(2-METHYLBIPHENYL-2-YL)METHYL~~]~~AMINO}PYRAZIN-2-YL)-L-PHENYLALANINE'>ML4</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.92Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[3hf6\|3hf6]], [[3hf8\|3hf8]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=ML4:4-(5-{[(2-METHYLBIPHENYL-2-YL)METHYL]AMINO}PYRAZIN-2-YL)-L-PHENYLALANINE'>ML4</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Tryptophan_5~~-~~monooxygenase Tryptophan~~ 5-~~monooxygenase], with EC number~~ [~~https://www.brenda~~-~~enzymes.info/php/result_flat.php4?ecno=1.14.16.4 1.14.16.4~~] </~~span~~></td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hfb OCA], [https://pdbe.org/3hfb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hfb RCSB], [https://www.ebi.ac.uk/pdbsum/3hfb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hfb ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hfb OCA], [https://pdbe.org/3hfb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hfb RCSB], [https://www.ebi.ac.uk/pdbsum/3hfb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hfb ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/TPH1_HUMAN TPH1_HUMAN]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 19:		Line 20:
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3hfb ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3hfb ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Trytophan Hydroxylase Type I (TPH1), most abundantly expressed in the gastrointestinal tract, initiates the synthesis of serotonin by catalyzing hydroxylation of tryptophan in the presence of biopterin and oxygen. We have previously described three series of novel, periphery-specific TPH1 inhibitors that selectively deplete serotonin in the gastrointestinal tract. We have now determined co-crystal structures of TPH1 with three of these inhibitors at high resolution. Analysis of the structural data showed that each of the three inhibitors fills the tryptophan binding pocket of TPH1 without reaching into the binding site of the cofactor pterin, and induces major conformational changes of the enzyme. The enzyme-inhibitor complexes assume a compact conformation that is similar to the one in tryptophan complex. Kinetic analysis showed that all three inhibitors are competitive versus the substrate tryptophan, consistent with the structural data that the compounds occupy the tryptophan binding site. On the other hand, all three inhibitors appear to be uncompetitive versus the cofactor 6-methyltetrahydropterin, which is not only consistent with the structural data but also indicate that the hydroxylation reaction follows an ordered binding mechanism in which a productive complex is formed only if tryptophan binds only after pterin, similar to the kinetic mechanisms of tyrosine and phenylalanine hydroxylase.
-
-	Mechanism of Inhibition of Novel Tryptophan Hydroxylase Inhibitors Revealed by Co-crystal Structures and Kinetic Analysis.,Cianchetta G, Stouch T, Yu W, Shi ZC, Tari LW, Swanson RV, Hunter MJ, Hoffman ID, Liu Q Curr Chem Genomics. 2010 Apr 14;4:19-26. PMID:20556201<ref>PMID:20556201</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 3hfb" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Hydroxylases 3D structures\|Hydroxylases 3D structures]]		*[[Hydroxylases 3D structures\|Hydroxylases 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Tryptophan 5-monooxygenase]]~~	+	[[Category: Hunter MJ]]
-	[[Category: Hunter~~, M J~~]]	+	[[Category: Swanson RV]]
-	[[Category: Swanson~~, R V~~]]	+	[[Category: Tari LW]]
-	[[Category: Tari~~, L W]]~~	+
-	~~[[Category: Iron]]~~	+
-	~~[[Category: Metal-binding]]~~	+
-	~~[[Category: Monooxygenase]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Phosphoprotein]]~~	+
-	~~[[Category: Serotonin biosynthesis]]~~	+
-	~~[[Category: Tryptophan hydroxylase type 1~~]]	+

OCA at 11:58, 13 October 2021

OCA — Wed, 13 Oct 2021 11:58:47 GMT

←Older revision		Revision as of 11:58, 13 October 2021
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	<StructureSection load='3hfb' size='340' side='right'caption='[[3hfb]], [[Resolution\|resolution]] 1.92Å' scene=''>		<StructureSection load='3hfb' size='340' side='right'caption='[[3hfb]], [[Resolution\|resolution]] 1.92Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3hfb]] is a 1 chain structure with 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=3HFB OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=3HFB FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3hfb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HFB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HFB FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=ML4:4-(5-{[(2-METHYLBIPHENYL-2-YL)METHYL]AMINO}PYRAZIN-2-YL)-L-PHENYLALANINE'>ML4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=ML4:4-(5-{[(2-METHYLBIPHENYL-2-YL)METHYL]AMINO}PYRAZIN-2-YL)-L-PHENYLALANINE'>ML4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3hf6\|3hf6]], [[3hf8\|3hf8]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3hf6\|3hf6]], [[3hf8\|3hf8]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Tryptophan_5-monooxygenase Tryptophan 5-monooxygenase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.16.4 1.14.16.4] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Tryptophan_5-monooxygenase Tryptophan 5-monooxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.16.4 1.14.16.4] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=3hfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hfb OCA], [~~http~~://pdbe.org/3hfb PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3hfb RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3hfb PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3hfb ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hfb OCA], [https://pdbe.org/3hfb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hfb RCSB], [https://www.ebi.ac.uk/pdbsum/3hfb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hfb ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==

OCA at 10:47, 16 September 2020

OCA — Wed, 16 Sep 2020 10:47:28 GMT

←Older revision		Revision as of 10:47, 16 September 2020
Line 1:		Line 1:

	==Crystal structure of human tryoptophan hydroxylase type 1 with LP-534193==		==Crystal structure of human tryoptophan hydroxylase type 1 with LP-534193==
-	<StructureSection load='3hfb' size='340' side='right' caption='[[3hfb]], [[Resolution\|resolution]] 1.92Å' scene=''>	+	<StructureSection load='3hfb' size='340' side='right'caption='[[3hfb]], [[Resolution\|resolution]] 1.92Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3hfb]] is a 1 chain structure with 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=3HFB OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3HFB FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3hfb]] is a 1 chain structure with 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=3HFB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3HFB FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=ML4:4-(5-{[(2-METHYLBIPHENYL-2-YL)METHYL]AMINO}PYRAZIN-2-YL)-L-PHENYLALANINE'>ML4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=ML4:4-(5-{[(2-METHYLBIPHENYL-2-YL)METHYL]AMINO}PYRAZIN-2-YL)-L-PHENYLALANINE'>ML4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3hf6\|3hf6]], [[3hf8\|3hf8]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3hf6\|3hf6]], [[3hf8\|3hf8]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptophan_5-monooxygenase Tryptophan 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.16.4 1.14.16.4] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptophan_5-monooxygenase Tryptophan 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.16.4 1.14.16.4] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3hfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hfb OCA], [http://pdbe.org/3hfb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hfb RCSB], [http://www.ebi.ac.uk/pdbsum/3hfb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hfb ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3hfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hfb OCA], [http://pdbe.org/3hfb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hfb RCSB], [http://www.ebi.ac.uk/pdbsum/3hfb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hfb ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 30:		Line 30:

	==See Also==		==See Also==
-	*[[~~Hydroxylase~~\|~~Hydroxylase~~]]	+	*[[Hydroxylases 3D structures\|Hydroxylases 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 36:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
		+	[[Category: Large Structures]]
	[[Category: Tryptophan 5-monooxygenase]]		[[Category: Tryptophan 5-monooxygenase]]
	[[Category: Hunter, M J]]		[[Category: Hunter, M J]]

OCA at 07:42, 12 December 2018

OCA — Wed, 12 Dec 2018 07:42:26 GMT

←Older revision		Revision as of 07:42, 12 December 2018
Line 1:		Line 1:
		+
	==Crystal structure of human tryoptophan hydroxylase type 1 with LP-534193==		==Crystal structure of human tryoptophan hydroxylase type 1 with LP-534193==
	<StructureSection load='3hfb' size='340' side='right' caption='[[3hfb]], [[Resolution\|resolution]] 1.92Å' scene=''>		<StructureSection load='3hfb' size='340' side='right' caption='[[3hfb]], [[Resolution\|resolution]] 1.92Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3hf6\|3hf6]], [[3hf8\|3hf8]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3hf6\|3hf6]], [[3hf8\|3hf8]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptophan_5-monooxygenase Tryptophan 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.16.4 1.14.16.4] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptophan_5-monooxygenase Tryptophan 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.16.4 1.14.16.4] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3hfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hfb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hfb RCSB], [http://www.ebi.ac.uk/pdbsum/3hfb PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3hfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hfb OCA], [http://pdbe.org/3hfb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hfb RCSB], [http://www.ebi.ac.uk/pdbsum/3hfb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hfb ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 12:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hf/3hfb_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hf/3hfb_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3hfb ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 26:		Line 27:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3hfb" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
-	*[[~~Tryptophan hydroxylase~~\|~~Tryptophan hydroxylase~~]]	+	*[[Hydroxylase\|Hydroxylase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:49, 8 December 2014

OCA — Mon, 08 Dec 2014 08:49:56 GMT

←Older revision		Revision as of 08:49, 8 December 2014
Line 1:		Line 1:
-	[[~~Image:~~3hfb.~~png~~\|~~left~~\|200px]]	+	==Crystal structure of human tryoptophan hydroxylase type 1 with LP-534193==
		+	<StructureSection load='3hfb' size='340' side='right' caption='[[3hfb]], [[Resolution\|resolution]] 1.92Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3hfb]] is a 1 chain structure with 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=3HFB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HFB FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=ML4:4-(5-{[(2-METHYLBIPHENYL-2-YL)METHYL]AMINO}PYRAZIN-2-YL)-L-PHENYLALANINE'>ML4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3hf6\|3hf6]], [[3hf8\|3hf8]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptophan_5-monooxygenase Tryptophan 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.16.4 1.14.16.4] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3hfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hfb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hfb RCSB], [http://www.ebi.ac.uk/pdbsum/3hfb PDBsum]</span></td></tr>
		+	</table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hf/3hfb_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Trytophan Hydroxylase Type I (TPH1), most abundantly expressed in the gastrointestinal tract, initiates the synthesis of serotonin by catalyzing hydroxylation of tryptophan in the presence of biopterin and oxygen. We have previously described three series of novel, periphery-specific TPH1 inhibitors that selectively deplete serotonin in the gastrointestinal tract. We have now determined co-crystal structures of TPH1 with three of these inhibitors at high resolution. Analysis of the structural data showed that each of the three inhibitors fills the tryptophan binding pocket of TPH1 without reaching into the binding site of the cofactor pterin, and induces major conformational changes of the enzyme. The enzyme-inhibitor complexes assume a compact conformation that is similar to the one in tryptophan complex. Kinetic analysis showed that all three inhibitors are competitive versus the substrate tryptophan, consistent with the structural data that the compounds occupy the tryptophan binding site. On the other hand, all three inhibitors appear to be uncompetitive versus the cofactor 6-methyltetrahydropterin, which is not only consistent with the structural data but also indicate that the hydroxylation reaction follows an ordered binding mechanism in which a productive complex is formed only if tryptophan binds only after pterin, similar to the kinetic mechanisms of tyrosine and phenylalanine hydroxylase.

-	~~{{STRUCTURE_3hfb\| PDB=3hfb \| SCENE= }}~~	+	Mechanism of Inhibition of Novel Tryptophan Hydroxylase Inhibitors Revealed by Co-crystal Structures and Kinetic Analysis.,Cianchetta G, Stouch T, Yu W, Shi ZC, Tari LW, Swanson RV, Hunter MJ, Hoffman ID, Liu Q Curr Chem Genomics. 2010 Apr 14;4:19-26. PMID:20556201<ref>PMID:20556201</ref>

-	~~===Crystal structure~~ of ~~human tryoptophan hydroxylase type 1 with LP-534193===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_20556201}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3hfb]] is a 1 chain structure with 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=3HFB OCA].~~	+

	==See Also==		==See Also==
	*[[Tryptophan hydroxylase\|Tryptophan hydroxylase]]		*[[Tryptophan hydroxylase\|Tryptophan hydroxylase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:020556201<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Tryptophan 5-monooxygenase]]		[[Category: Tryptophan 5-monooxygenase]]
-	[[Category: Hunter, M J.]]	+	[[Category: Hunter, M J]]
-	[[Category: Swanson, R V.]]	+	[[Category: Swanson, R V]]
-	[[Category: Tari, L W.]]	+	[[Category: Tari, L W]]
	[[Category: Iron]]		[[Category: Iron]]
	[[Category: Metal-binding]]		[[Category: Metal-binding]]

OCA at 14:43, 20 October 2012

OCA — Sat, 20 Oct 2012 14:43:22 GMT

←Older revision		Revision as of 14:43, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3hfb]] is a 1 chain structure ~~of [[Tryptophan hydroxylase]]~~ with 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=3HFB OCA].	+	[[3hfb]] is a 1 chain structure with 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=3HFB OCA].

	==See Also==		==See Also==

OCA at 16:02, 26 July 2012

OCA — Thu, 26 Jul 2012 16:02:18 GMT

←Older revision		Revision as of 16:02, 26 July 2012
Line 1:		Line 1:
	[[Image:3hfb.png\|left\|200px]]		[[Image:3hfb.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3hfb", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3hfb\| PDB=3hfb \| SCENE= }}		{{STRUCTURE_3hfb\| PDB=3hfb \| SCENE= }}

	===Crystal structure of human tryoptophan hydroxylase type 1 with LP-534193===		===Crystal structure of human tryoptophan hydroxylase type 1 with LP-534193===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_20556201}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 20556201 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_20556201}}		{{ABSTRACT_PUBMED_20556201}}

Line 22:		Line 11:

	==See Also==		==See Also==
-	*[[Tryptophan hydroxylase]]	+	*[[Tryptophan hydroxylase\|Tryptophan hydroxylase]]

	==Reference==		==Reference==

OCA at 06:32, 28 March 2012

OCA — Wed, 28 Mar 2012 06:32:50 GMT

←Older revision		Revision as of 06:32, 28 March 2012
Line 11:		Line 11:
	===Crystal structure of human tryoptophan hydroxylase type 1 with LP-534193===		===Crystal structure of human tryoptophan hydroxylase type 1 with LP-534193===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_20556201}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 20556201 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_20556201}}

	==About this Structure==		==About this Structure==
-	[[3hfb]] is a 1 chain structure with 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=3HFB OCA].	+	[[3hfb]] is a 1 chain structure of [[Tryptophan hydroxylase]] with 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=3HFB OCA].

	==See Also==		==See Also==
	*[[Tryptophan hydroxylase]]		*[[Tryptophan hydroxylase]]
		+
		+	==Reference==
		+	<ref group="xtra">PMID:020556201</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Tryptophan 5-monooxygenase]]		[[Category: Tryptophan 5-monooxygenase]]
Line 22:		Line 31:
	[[Category: Swanson, R V.]]		[[Category: Swanson, R V.]]
	[[Category: Tari, L W.]]		[[Category: Tari, L W.]]
-	[[Category: Alternative splicing]]
	[[Category: Iron]]		[[Category: Iron]]
	[[Category: Metal-binding]]		[[Category: Metal-binding]]

OCA: Protected "3hfb" [edit=sysop:move=sysop]

OCA — Sun, 02 Jan 2011 03:20:11 GMT

Protected "3hfb" [edit=sysop:move=sysop]

←Older revision

Revision as of 03:20, 2 January 2011

OCA at 03:20, 2 January 2011

OCA — Sun, 02 Jan 2011 03:20:09 GMT

←Older revision		Revision as of 03:20, 2 January 2011
Line 1:		Line 1:
-	{{Seed}}
	[[Image:3hfb.png\|left\|200px]]		[[Image:3hfb.png\|left\|200px]]

Line 14:		Line 13:

	==About this Structure==		==About this Structure==
-	~~3HFB~~ is a 1 chain structure with 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=3HFB OCA].	+	[[3hfb]] is a 1 chain structure with 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=3HFB OCA].
		+
		+	==See Also==
		+	*[[Tryptophan hydroxylase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Tryptophan 5-monooxygenase]]		[[Category: Tryptophan 5-monooxygenase]]
Line 28:		Line 30:
	[[Category: Serotonin biosynthesis]]		[[Category: Serotonin biosynthesis]]
	[[Category: Tryptophan hydroxylase type 1]]		[[Category: Tryptophan hydroxylase type 1]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 27 10:27:50 2010''