1dro - Revision history

OCA at 08:24, 22 May 2024

2024-05-22T08:24:57Z

←Older revision		Revision as of 08:24, 22 May 2024
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=1dro 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=1dro ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	BACKGROUND: The pleckstrin homology (PH) domain, which is approximately 100 amino acids long, has been found in about 70 proteins involved in signal transduction and cytoskeletal function, a frequency comparable to SH2 (src homology 2) and SH3 domains. PH domains have been shown to bind the beta gamma-subunits of G-proteins and phosphatidylinositol 4,5-bisphosphate (PIP2). It is conceivable that the PH domain of beta-spectrin plays a part in the association of spectrin with the plasma membrane of cells. RESULTS: We have solved the solution structure of the 122-residue PH domain of Drosophila beta-spectrin. The overall fold consists of two antiparallel beta-sheets packing against each other at an angle of approximately 60 degrees to form a beta-sandwich, a two-turn alpha-helix unique to spectrin PH domains, and a four-turn C-terminal alpha-helix. One of the major insertions in beta-spectrin PH domains forms a long, basic surface loop and appears to undergo slow conformational exchange in solution. This loop shows big spectral changes upon addition of D-myo-inositol 1,4,5-trisphosphate (IP3). CONCLUSIONS: We propose that the groove at the outer surface of the second beta-sheet is an important site of association with other proteins. This site and the possible lipid-binding site can serve to localize the spectrin network under the plasma membrane. More generally, it has to be considered that the common fold observed for the PH domain structures solved so far does not necessarily mean that all PH domains have similar functions. In fact, the residues constituting potential binding sites for ligands or other proteins are only slightly conserved between different PH domains.
		+
		+	Solution structure of the pleckstrin homology domain of Drosophila beta-spectrin.,Zhang P, Talluri S, Deng H, Branton D, Wagner G Structure. 1995 Nov 15;3(11):1185-95. PMID:8591029<ref>PMID:8591029</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 1dro" style="background-color:#fffaf0;"></div>

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

OCA at 09:52, 20 March 2024

2024-03-20T09:52:58Z

←Older revision		Revision as of 09:52, 20 March 2024
Line 1:		Line 1:

	==NMR STRUCTURE OF THE CYTOSKELETON/SIGNAL TRANSDUCTION PROTEIN==		==NMR STRUCTURE OF THE CYTOSKELETON/SIGNAL TRANSDUCTION PROTEIN==
-	<StructureSection load='1dro' size='340' side='right'caption='[[1dro~~]], [[NMR_Ensembles_of_Models \| 15 NMR models~~]]' scene=''>	+	<StructureSection load='1dro' size='340' side='right'caption='[[1dro]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1dro]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Drome Drome~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DRO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DRO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1dro]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DRO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DRO FirstGlance]. <br>
-	</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=1dro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dro OCA], [https://pdbe.org/1dro PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dro RCSB], [https://www.ebi.ac.uk/pdbsum/1dro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dro ProSAT]</span></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=1dro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dro OCA], [https://pdbe.org/1dro PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dro RCSB], [https://www.ebi.ac.uk/pdbsum/1dro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dro ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/SPTCB_DROME SPTCB_DROME]] Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. Interacts with calmodulin in a calcium-dependent manner.<ref>PMID:3680372</ref>	+	[https://www.uniprot.org/uniprot/SPTCB_DROME SPTCB_DROME] Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. Interacts with calmodulin in a calcium-dependent manner.<ref>PMID:3680372</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 18:		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=1dro 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=1dro ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	BACKGROUND: The pleckstrin homology (PH) domain, which is approximately 100 amino acids long, has been found in about 70 proteins involved in signal transduction and cytoskeletal function, a frequency comparable to SH2 (src homology 2) and SH3 domains. PH domains have been shown to bind the beta gamma-subunits of G-proteins and phosphatidylinositol 4,5-bisphosphate (PIP2). It is conceivable that the PH domain of beta-spectrin plays a part in the association of spectrin with the plasma membrane of cells. RESULTS: We have solved the solution structure of the 122-residue PH domain of Drosophila beta-spectrin. The overall fold consists of two antiparallel beta-sheets packing against each other at an angle of approximately 60 degrees to form a beta-sandwich, a two-turn alpha-helix unique to spectrin PH domains, and a four-turn C-terminal alpha-helix. One of the major insertions in beta-spectrin PH domains forms a long, basic surface loop and appears to undergo slow conformational exchange in solution. This loop shows big spectral changes upon addition of D-myo-inositol 1,4,5-trisphosphate (IP3). CONCLUSIONS: We propose that the groove at the outer surface of the second beta-sheet is an important site of association with other proteins. This site and the possible lipid-binding site can serve to localize the spectrin network under the plasma membrane. More generally, it has to be considered that the common fold observed for the PH domain structures solved so far does not necessarily mean that all PH domains have similar functions. In fact, the residues constituting potential binding sites for ligands or other proteins are only slightly conserved between different PH domains.
-
-	Solution structure of the pleckstrin homology domain of Drosophila beta-spectrin.,Zhang P, Talluri S, Deng H, Branton D, Wagner G Structure. 1995 Nov 15;3(11):1185-95. PMID:8591029<ref>PMID:8591029</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1dro" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
-	*[[Spectrin\|Spectrin]]	+	*[[Spectrin 3D structures\|Spectrin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Drome~~]]	+	[[Category: Drosophila melanogaster]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Branton, D]]	+	[[Category: Branton D]]
-	[[Category: Deng, H]]	+	[[Category: Deng H]]
-	[[Category: Talluri, S]]	+	[[Category: Talluri S]]
-	[[Category: Wagner, G]]	+	[[Category: Wagner G]]
-	[[Category: Zhang, P]]	+	[[Category: Zhang P]]
-	~~[[Category: Cytoskeleton~~]]	+

OCA at 09:30, 21 July 2021

2021-07-21T09:30:37Z

←Older revision		Revision as of 09:30, 21 July 2021
Line 3:		Line 3:
	<StructureSection load='1dro' size='340' side='right'caption='[[1dro]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>		<StructureSection load='1dro' size='340' side='right'caption='[[1dro]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1dro]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Drome Drome]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DRO OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1DRO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1dro]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DRO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DRO FirstGlance]. <br>
-	</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=1dro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dro OCA], [~~http~~://pdbe.org/1dro PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1dro RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1dro PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1dro ProSAT]</span></td></tr>	+	</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=1dro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dro OCA], [https://pdbe.org/1dro PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dro RCSB], [https://www.ebi.ac.uk/pdbsum/1dro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dro ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/SPTCB_DROME SPTCB_DROME]] Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. Interacts with calmodulin in a calcium-dependent manner.<ref>PMID:3680372</ref>	+	[[https://www.uniprot.org/uniprot/SPTCB_DROME SPTCB_DROME]] Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. Interacts with calmodulin in a calcium-dependent manner.<ref>PMID:3680372</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 14:43, 16 October 2019

2019-10-16T14:43:38Z

←Older revision		Revision as of 14:43, 16 October 2019
Line 1:		Line 1:

	==NMR STRUCTURE OF THE CYTOSKELETON/SIGNAL TRANSDUCTION PROTEIN==		==NMR STRUCTURE OF THE CYTOSKELETON/SIGNAL TRANSDUCTION PROTEIN==
-	<StructureSection load='1dro' size='340' side='right' caption='[[1dro]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>	+	<StructureSection load='1dro' size='340' side='right'caption='[[1dro]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1dro]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DRO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DRO FirstGlance]. <br>		<table><tr><td colspan='2'>[[1dro]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DRO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DRO FirstGlance]. <br>
Line 27:		Line 27:
	</div>		</div>
	<div class="pdbe-citations 1dro" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1dro" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Spectrin\|Spectrin]]
	== References ==		== References ==
	<references/>		<references/>
Line 32:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Drome]]		[[Category: Drome]]
		+	[[Category: Large Structures]]
	[[Category: Branton, D]]		[[Category: Branton, D]]
	[[Category: Deng, H]]		[[Category: Deng, H]]

OCA at 08:04, 13 December 2017

2017-12-13T08:04:45Z

←Older revision		Revision as of 08:04, 13 December 2017
Line 1:		Line 1:
		+
	==NMR STRUCTURE OF THE CYTOSKELETON/SIGNAL TRANSDUCTION PROTEIN==		==NMR STRUCTURE OF THE CYTOSKELETON/SIGNAL TRANSDUCTION PROTEIN==
	<StructureSection load='1dro' size='340' side='right' caption='[[1dro]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>		<StructureSection load='1dro' size='340' side='right' caption='[[1dro]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1dro]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DRO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DRO FirstGlance]. <br>		<table><tr><td colspan='2'>[[1dro]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DRO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DRO FirstGlance]. <br>
-	</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=1dro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dro OCA], [http://pdbe.org/1dro PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dro RCSB], [http://www.ebi.ac.uk/pdbsum/1dro PDBsum]</span></td></tr>	+	</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=1dro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dro OCA], [http://pdbe.org/1dro PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dro RCSB], [http://www.ebi.ac.uk/pdbsum/1dro PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dro ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 11:		Line 12:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dr/1dro_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dr/1dro_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>
Line 26:		Line 27:
	</div>		</div>
	<div class="pdbe-citations 1dro" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1dro" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Spectrin\|Spectrin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 03:30, 8 February 2016

2016-02-08T03:30:03Z

←Older revision		Revision as of 03:30, 8 February 2016
Line 15:		Line 15:
	<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=1dro ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 07:26, 10 September 2015

2015-09-10T07:26:31Z

←Older revision		Revision as of 07:26, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1dro' size='340' side='right' caption='[[1dro]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>		<StructureSection load='1dro' size='340' side='right' caption='[[1dro]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1dro]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Drosophila_melanogaster Drosophila melanogaster~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DRO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DRO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1dro]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DRO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DRO FirstGlance]. <br>
-	</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=1dro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dro OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dro RCSB], [http://www.ebi.ac.uk/pdbsum/1dro PDBsum]</span></td></tr>	+	</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=1dro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dro OCA], [http://pdbe.org/1dro PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dro RCSB], [http://www.ebi.ac.uk/pdbsum/1dro PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 25:		Line 25:
	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 1dro" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 32:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Drosophila melanogaster~~]]	+	[[Category: Drome]]
	[[Category: Branton, D]]		[[Category: Branton, D]]
	[[Category: Deng, H]]		[[Category: Deng, H]]

OCA at 20:15, 24 December 2014

2014-12-24T20:15:00Z

←Older revision		Revision as of 20:15, 24 December 2014
Line 5:		Line 5:
	</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=1dro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dro OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dro RCSB], [http://www.ebi.ac.uk/pdbsum/1dro PDBsum]</span></td></tr>		</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=1dro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dro OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dro RCSB], [http://www.ebi.ac.uk/pdbsum/1dro PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SPTCB_DROME SPTCB_DROME]] Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. Interacts with calmodulin in a calcium-dependent manner.<ref>PMID:3680372</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 22:29, 22 December 2014

2014-12-22T22:29:23Z

←Older revision		Revision as of 22:29, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1dro]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DRO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DRO FirstGlance]. <br>		<table><tr><td colspan='2'>[[1dro]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DRO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DRO FirstGlance]. <br>
-	</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=1dro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dro OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dro RCSB], [http://www.ebi.ac.uk/pdbsum/1dro PDBsum]</span></td></tr>	+	</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=1dro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dro OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dro RCSB], [http://www.ebi.ac.uk/pdbsum/1dro PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</StructureSection>		</StructureSection>
	[[Category: Drosophila melanogaster]]		[[Category: Drosophila melanogaster]]
-	[[Category: Branton, D.]]	+	[[Category: Branton, D]]
-	[[Category: Deng, H.]]	+	[[Category: Deng, H]]
-	[[Category: Talluri, S.]]	+	[[Category: Talluri, S]]
-	[[Category: Wagner, G.]]	+	[[Category: Wagner, G]]
-	[[Category: Zhang, P.]]	+	[[Category: Zhang, P]]
	[[Category: Cytoskeleton]]		[[Category: Cytoskeleton]]

OCA at 10:57, 10 September 2014

2014-09-10T10:57:10Z

←Older revision		Revision as of 10:57, 10 September 2014
Line 1:		Line 1:
-	[[~~Image~~:1dro.~~png\|left~~\|200px]]	+	==NMR STRUCTURE OF THE CYTOSKELETON/SIGNAL TRANSDUCTION PROTEIN==
		+	<StructureSection load='1dro' size='340' side='right' caption='[[1dro]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1dro]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DRO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DRO FirstGlance]. <br>
		+	</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=1dro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dro OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dro RCSB], [http://www.ebi.ac.uk/pdbsum/1dro 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/dr/1dro_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 ==
		+	BACKGROUND: The pleckstrin homology (PH) domain, which is approximately 100 amino acids long, has been found in about 70 proteins involved in signal transduction and cytoskeletal function, a frequency comparable to SH2 (src homology 2) and SH3 domains. PH domains have been shown to bind the beta gamma-subunits of G-proteins and phosphatidylinositol 4,5-bisphosphate (PIP2). It is conceivable that the PH domain of beta-spectrin plays a part in the association of spectrin with the plasma membrane of cells. RESULTS: We have solved the solution structure of the 122-residue PH domain of Drosophila beta-spectrin. The overall fold consists of two antiparallel beta-sheets packing against each other at an angle of approximately 60 degrees to form a beta-sandwich, a two-turn alpha-helix unique to spectrin PH domains, and a four-turn C-terminal alpha-helix. One of the major insertions in beta-spectrin PH domains forms a long, basic surface loop and appears to undergo slow conformational exchange in solution. This loop shows big spectral changes upon addition of D-myo-inositol 1,4,5-trisphosphate (IP3). CONCLUSIONS: We propose that the groove at the outer surface of the second beta-sheet is an important site of association with other proteins. This site and the possible lipid-binding site can serve to localize the spectrin network under the plasma membrane. More generally, it has to be considered that the common fold observed for the PH domain structures solved so far does not necessarily mean that all PH domains have similar functions. In fact, the residues constituting potential binding sites for ligands or other proteins are only slightly conserved between different PH domains.

-	~~{{STRUCTURE_1dro\| PDB=1dro \| SCENE= }}~~	+	Solution structure of the pleckstrin homology domain of Drosophila beta-spectrin.,Zhang P, Talluri S, Deng H, Branton D, Wagner G Structure. 1995 Nov 15;3(11):1185-95. PMID:8591029<ref>PMID:8591029</ref>

-	~~===NMR STRUCTURE OF THE CYTOSKELETON~~/~~SIGNAL TRANSDUCTION PROTEIN===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_8591029}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1dro]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Drosophila_melanogaster Drosophila melanogaster]~~. ~~Full experimental information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1DRO OCA].~~	+

	==See Also==		==See Also==
	*[[Spectrin\|Spectrin]]		*[[Spectrin\|Spectrin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:008591029<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Drosophila melanogaster]]		[[Category: Drosophila melanogaster]]
	[[Category: Branton, D.]]		[[Category: Branton, D.]]