1xfr - Revision history

OCA at 14:07, 9 May 2024

2024-05-09T14:07:54Z

←Older revision		Revision as of 14:07, 9 May 2024
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	==Solution structure of the Bombyx mori pheromone-binding protein fragment BmPBP(1-128) at pH 6.5==		==Solution structure of the Bombyx mori pheromone-binding protein fragment BmPBP(1-128) at pH 6.5==
-	<StructureSection load='1xfr' size='340' side='right'caption='[[1xfr~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>	+	<StructureSection load='1xfr' size='340' side='right'caption='[[1xfr]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1xfr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Bommo Bommo~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XFR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XFR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1xfr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XFR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XFR FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style~~=~~'overflow: auto; max-height: 3em;'>[[1ls8\|1ls8]], [[1dqe\|1dqe]], [[1gm0\|1gm0]]</div~~></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1xfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xfr OCA], [https://pdbe.org/1xfr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xfr RCSB], [https://www.ebi.ac.uk/pdbsum/1xfr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xfr 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=1xfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xfr OCA], [https://pdbe.org/1xfr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xfr RCSB], [https://www.ebi.ac.uk/pdbsum/1xfr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xfr ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PBP_BOMMO PBP_BOMMO]] This major soluble protein in olfactory sensilla of male moths serves to solubilize the extremely hydrophobic pheromone molecules such as bombykol and to transport pheromone through the aqueous lymph to receptors located on olfactory cilia.	+	[https://www.uniprot.org/uniprot/PBP_BOMMO PBP_BOMMO] This major soluble protein in olfactory sensilla of male moths serves to solubilize the extremely hydrophobic pheromone molecules such as bombykol and to transport pheromone through the aqueous lymph to receptors located on olfactory cilia.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bommo~~]]	+	[[Category: Bombyx mori]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Damberger~~, F F~~]]	+	[[Category: Damberger FF]]
-	[[Category: Leal~~, W S~~]]	+	[[Category: Leal WS]]
-	[[Category: Michel, E]]	+	[[Category: Michel E]]
-	[[Category: Wuthrich, K]]	+	[[Category: Wuthrich K]]
-	~~[[Category: Alpha-helical transport protein]]~~	+
-	~~[[Category: Bmpbpb]]~~	+
-	~~[[Category: Bombyx mori pheromone-binding protein]]~~	+
-	~~[[Category: Insect odorant-binding protein]]~~	+
-	~~[[Category: Transport protein~~]]	+

OCA at 07:41, 16 March 2022

2022-03-16T07:41:09Z

←Older revision		Revision as of 07:41, 16 March 2022
Line 3:		Line 3:
	<StructureSection load='1xfr' size='340' side='right'caption='[[1xfr]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='1xfr' size='340' side='right'caption='[[1xfr]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1xfr]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Bommo Bommo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XFR OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1XFR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1xfr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bommo Bommo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XFR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XFR FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ls8\|1ls8]], [[1dqe\|1dqe]], [[1gm0\|1gm0]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ls8\|1ls8]], [[1dqe\|1dqe]], [[1gm0\|1gm0]]</div></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=1xfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xfr OCA], [~~http~~://pdbe.org/1xfr PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1xfr RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1xfr PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1xfr 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=1xfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xfr OCA], [https://pdbe.org/1xfr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xfr RCSB], [https://www.ebi.ac.uk/pdbsum/1xfr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xfr ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PBP_BOMMO PBP_BOMMO]] This major soluble protein in olfactory sensilla of male moths serves to solubilize the extremely hydrophobic pheromone molecules such as bombykol and to transport pheromone through the aqueous lymph to receptors located on olfactory cilia.	+	[[https://www.uniprot.org/uniprot/PBP_BOMMO PBP_BOMMO]] This major soluble protein in olfactory sensilla of male moths serves to solubilize the extremely hydrophobic pheromone molecules such as bombykol and to transport pheromone through the aqueous lymph to receptors located on olfactory cilia.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 07:03, 10 June 2020

2020-06-10T07:03:32Z

←Older revision		Revision as of 07:03, 10 June 2020
Line 1:		Line 1:

	==Solution structure of the Bombyx mori pheromone-binding protein fragment BmPBP(1-128) at pH 6.5==		==Solution structure of the Bombyx mori pheromone-binding protein fragment BmPBP(1-128) at pH 6.5==
-	<StructureSection load='1xfr' size='340' side='right' caption='[[1xfr]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>	+	<StructureSection load='1xfr' size='340' side='right'caption='[[1xfr]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1xfr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bommo Bommo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XFR OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1XFR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1xfr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bommo Bommo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XFR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1XFR FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ls8\|1ls8]], [[1dqe\|1dqe]], [[1gm0\|1gm0]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ls8\|1ls8]], [[1dqe\|1dqe]], [[1gm0\|1gm0]]</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=1xfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xfr OCA], [http://pdbe.org/1xfr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xfr RCSB], [http://www.ebi.ac.uk/pdbsum/1xfr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xfr 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=1xfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xfr OCA], [http://pdbe.org/1xfr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xfr RCSB], [http://www.ebi.ac.uk/pdbsum/1xfr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xfr ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 36:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Bommo]]		[[Category: Bommo]]
		+	[[Category: Large Structures]]
	[[Category: Damberger, F F]]		[[Category: Damberger, F F]]
	[[Category: Leal, W S]]		[[Category: Leal, W S]]

OCA at 10:16, 5 September 2018

2018-09-05T10:16:44Z

←Older revision		Revision as of 10:16, 5 September 2018
Line 19:		Line 19:
	</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=1xfr 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=1xfr ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The Bombyx mori pheromone-binding protein (BmorPBP) undergoes a pH-dependent conformational transition from a form at basic pH, which contains an open cavity suitable for ligand binding (BmorPBP(B)), to a form at pH 4.5, where this cavity is occupied by an additional helix (BmorPBP(A)). This helix alpha7 is formed by the C-terminal dodecapeptide 131-142, which is flexibly disordered on the protein surface in BmorPBP(B) and in its complex with the pheromone bombykol. Previous work showed that the ligand-binding cavity cannot accommodate both bombykol and helix alpha7. Here we further investigated mechanistic aspects of the physiologically crucial ejection of the ligand at lower pH values by solution NMR studies of the variant protein BmorPBP(1-128), where the C-terminal helix-forming tetradecapeptide is removed. The NMR structure of the truncated protein at pH 6.5 corresponds closely to BmorPBP(B). At pH 4.5, BmorPBP(1-128) maintains a B-type structure that is in a slow equilibrium, on the NMR chemical shift timescale, with a low-pH conformation for which a discrete set of (15)N-(1)H correlation peaks is NMR unobservable. The full NMR spectrum was recovered upon readjusting the pH of the protein solution to 6.5. These data reveal dual roles for the C-terminal tetradecapeptide of BmorPBP in the mechanism of reversible pheromone binding and transport, where it governs dynamic equilibria between two locally different protein conformations at acidic pH and competes with the ligand for binding to the interior cavity.
		+
		+	Dynamic conformational equilibria in the physiological function of the Bombyx mori pheromone-binding protein.,Michel E, Damberger FF, Ishida Y, Fiorito F, Lee D, Leal WS, Wuthrich K J Mol Biol. 2011 May 20;408(5):922-31. Epub 2011 Mar 17. PMID:21396939<ref>PMID:21396939</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 1xfr" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Pheromone binding protein\|Pheromone binding protein]]		*[[Pheromone binding protein\|Pheromone binding protein]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 07:17, 18 April 2018

2018-04-18T07:17:04Z

←Older revision		Revision as of 07:17, 18 April 2018
Line 1:		Line 1:
		+
	==Solution structure of the Bombyx mori pheromone-binding protein fragment BmPBP(1-128) at pH 6.5==		==Solution structure of the Bombyx mori pheromone-binding protein fragment BmPBP(1-128) at pH 6.5==
	<StructureSection load='1xfr' size='340' side='right' caption='[[1xfr]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='1xfr' size='340' side='right' caption='[[1xfr]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1xfr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bommo Bommo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XFR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XFR FirstGlance]. <br>		<table><tr><td colspan='2'>[[1xfr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bommo Bommo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XFR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XFR FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ls8\|1ls8]], [[1dqe\|1dqe]], [[1gm0\|1gm0]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ls8\|1ls8]], [[1dqe\|1dqe]], [[1gm0\|1gm0]]</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=1xfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xfr OCA], [http://pdbe.org/1xfr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xfr RCSB], [http://www.ebi.ac.uk/pdbsum/1xfr 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=1xfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xfr OCA], [http://pdbe.org/1xfr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xfr RCSB], [http://www.ebi.ac.uk/pdbsum/1xfr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xfr ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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/xf/1xfr_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xf/1xfr_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>

OCA at 13:10, 7 February 2016

2016-02-07T13:10:07Z

←Older revision		Revision as of 13:10, 7 February 2016
Line 16:		Line 16:
	<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=1xfr ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>

OCA at 01:45, 10 September 2015

2015-09-10T01:45:47Z

←Older revision		Revision as of 01:45, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1xfr' size='340' side='right' caption='[[1xfr]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='1xfr' size='340' side='right' caption='[[1xfr]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1xfr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Bombyx_mori Bombyx mori~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XFR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XFR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1xfr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bommo Bommo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XFR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XFR FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ls8\|1ls8]], [[1dqe\|1dqe]], [[1gm0\|1gm0]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ls8\|1ls8]], [[1dqe\|1dqe]], [[1gm0\|1gm0]]</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=1xfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xfr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1xfr RCSB], [http://www.ebi.ac.uk/pdbsum/1xfr 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=1xfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xfr OCA], [http://pdbe.org/1xfr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xfr RCSB], [http://www.ebi.ac.uk/pdbsum/1xfr PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 18:
	</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/chain_selection.php?pdb_ID=2ata ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
		+
		+	==See Also==
		+	*[[Pheromone binding protein\|Pheromone binding protein]]
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bombyx mori~~]]	+	[[Category: Bommo]]
	[[Category: Damberger, F F]]		[[Category: Damberger, F F]]
	[[Category: Leal, W S]]		[[Category: Leal, W S]]

OCA at 15:19, 24 December 2014

2014-12-24T15:19:09Z

←Older revision		Revision as of 15:19, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1xfr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XFR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XFR FirstGlance]. <br>		<table><tr><td colspan='2'>[[1xfr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XFR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XFR FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ls8\|1ls8]], [[1dqe\|1dqe]], [[1gm0\|1gm0]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ls8\|1ls8]], [[1dqe\|1dqe]], [[1gm0\|1gm0]]</td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xfr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1xfr RCSB], [http://www.ebi.ac.uk/pdbsum/1xfr 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=1xfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xfr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1xfr RCSB], [http://www.ebi.ac.uk/pdbsum/1xfr PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PBP_BOMMO PBP_BOMMO]] This major soluble protein in olfactory sensilla of male moths serves to solubilize the extremely hydrophobic pheromone molecules such as bombykol and to transport pheromone through the aqueous lymph to receptors located on olfactory cilia.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 19:		Line 21:
	</StructureSection>		</StructureSection>
	[[Category: Bombyx mori]]		[[Category: Bombyx mori]]
-	[[Category: Damberger, F F.]]	+	[[Category: Damberger, F F]]
-	[[Category: Leal, W S.]]	+	[[Category: Leal, W S]]
-	[[Category: Michel, E.]]	+	[[Category: Michel, E]]
-	[[Category: Wuthrich, K.]]	+	[[Category: Wuthrich, K]]
	[[Category: Alpha-helical transport protein]]		[[Category: Alpha-helical transport protein]]
	[[Category: Bmpbpb]]		[[Category: Bmpbpb]]

OCA at 20:58, 29 September 2014

2014-09-29T20:58:41Z

←Older revision		Revision as of 20:58, 29 September 2014
Line 1:		Line 1:
-	~~[[Image:1xfr.png\|left\|200px]]~~	+	==Solution structure of the Bombyx mori pheromone-binding protein fragment BmPBP(1-128) at pH 6.5==
-		+	<StructureSection load='1xfr' size='340' side='right' caption='[[1xfr]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
-	~~{{STRUCTURE_1xfr\| PDB=1xfr \| SCENE= }}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[1xfr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XFR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XFR FirstGlance]. <br>
-	===Solution structure of the Bombyx mori pheromone-binding protein fragment BmPBP(1-128) at pH 6.5===	+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ls8\|1ls8]], [[1dqe\|1dqe]], [[1gm0\|1gm0]]</td></tr>
-		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xfr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1xfr RCSB], [http://www.ebi.ac.uk/pdbsum/1xfr PDBsum]</span></td></tr>
-	~~{{ABSTRACT_PUBMED_021396939}}~~	+	<table>
-		+	== Evolutionary Conservation ==
-	==~~About this Structure~~==	+	[[Image:Consurf_key_small.gif\|200px\|right]]
-	[[1xfr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XFR OCA].	+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xf/1xfr_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>
		+	__TOC__
		+	</StructureSection>
	[[Category: Bombyx mori]]		[[Category: Bombyx mori]]
	[[Category: Damberger, F F.]]		[[Category: Damberger, F F.]]

OCA: Protected "1xfr" [edit=sysop:move=sysop]

2013-01-05T11:57:04Z

Protected "1xfr" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:57, 5 January 2013