3r05 - Revision history

OCA at 12:04, 14 March 2024

OCA — Thu, 14 Mar 2024 12:04:30 GMT

←Older revision		Revision as of 12:04, 14 March 2024
Line 3:		Line 3:
	<StructureSection load='3r05' size='340' side='right'caption='[[3r05]], [[Resolution\|resolution]] 2.95Å' scene=''>		<StructureSection load='3r05' size='340' side='right'caption='[[3r05]], [[Resolution\|resolution]] 2.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3r05]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Bovin Bovin~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R05 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R05 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3r05]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R05 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R05 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=NAG:N~~-~~ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.95Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~NRXN1 ([https~~:/~~/www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=3r05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r05 OCA], [https://pdbe.org/3r05 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r05 RCSB], [https://www.ebi.ac.uk/pdbsum/3r05 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r05 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=3r05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r05 OCA], [https://pdbe.org/3r05 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r05 RCSB], [https://www.ebi.ac.uk/pdbsum/3r05 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r05 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/NRX1A_BOVIN NRX1A_BOVIN]] Cell surface protein involved in cell-cell-interactions, exocytosis of secretory granules and regulation of signal transmission. Function is isoform-specific. Alpha-type isoforms have a long N-terminus with six laminin G-like domains and play an important role in synaptic signal transmission. Alpha-type isoforms play a role in the regulation of calcium channel activity and Ca(2+)-triggered neurotransmitter release at synapses and at neuromuscular junctions. They play an important role in Ca(2+)-triggered exocytosis of secretory granules in pituitary gland. They may effect their functions at synapses and in endocrine cells via their interactions with proteins from the exocytotic machinery. Likewise, alpha-type isoforms play a role in regulating the activity of postsynaptic NMDA receptors, a subtype of glutamate-gated ion channels (By similarity). Both alpha-type and beta-type isoforms may play a role in the formation or maintenance of synaptic junctions via their interactions (via the extracellular domains) with neuroligin family members, CBLN1 or CBLN2. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses. Alpha-type isoforms were first identified as receptors for alpha-latrotoxin from spider venom.	+	[https://www.uniprot.org/uniprot/NRX1A_BOVIN NRX1A_BOVIN] Cell surface protein involved in cell-cell-interactions, exocytosis of secretory granules and regulation of signal transmission. Function is isoform-specific. Alpha-type isoforms have a long N-terminus with six laminin G-like domains and play an important role in synaptic signal transmission. Alpha-type isoforms play a role in the regulation of calcium channel activity and Ca(2+)-triggered neurotransmitter release at synapses and at neuromuscular junctions. They play an important role in Ca(2+)-triggered exocytosis of secretory granules in pituitary gland. They may effect their functions at synapses and in endocrine cells via their interactions with proteins from the exocytotic machinery. Likewise, alpha-type isoforms play a role in regulating the activity of postsynaptic NMDA receptors, a subtype of glutamate-gated ion channels (By similarity). Both alpha-type and beta-type isoforms may play a role in the formation or maintenance of synaptic junctions via their interactions (via the extracellular domains) with neuroligin family members, CBLN1 or CBLN2. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses. Alpha-type isoforms were first identified as receptors for alpha-latrotoxin from spider venom.
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	alpha-Neurexins are essential synaptic adhesion molecules implicated in autism spectrum disorder and schizophrenia. The alpha-neurexin extracellular domain consists of six LNS domains interspersed by three EGF-like repeats and interacts with many different proteins in the synaptic cleft. To understand how alpha-neurexins might function as synaptic organizers, we solved the structure of the neurexin 1alpha extracellular domain (n1alpha) to 2.65 A. The L-shaped molecule can be divided into a flexible repeat I (LNS1-EGF-A-LNS2), a rigid horseshoe-shaped repeat II (LNS3-EGF-B-LNS4) with structural similarity to so-called reelin repeats, and an extended repeat III (LNS5-EGF-B-LNS6) with controlled flexibility. A 2.95 A structure of n1alpha carrying splice insert SS#3 in LNS4 reveals that SS#3 protrudes as a loop and does not alter the rigid arrangement of repeat II. The global architecture imposed by conserved structural features enables alpha-neurexins to recruit and organize proteins in distinct and variable ways, influenced by splicing, thereby promoting synaptic function.	+
-		+
-	The structure of neurexin 1alpha reveals features promoting a role as synaptic organizer.,Chen F, Venugopal V, Murray B, Rudenko G Structure. 2011 Jun 8;19(6):779-89. Epub 2011 May 27. PMID:21620716<ref>PMID:21620716</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3r05" style="background-color:#fffaf0;"></div>~~	+

	==See Also==		==See Also==
	*[[Neurexin\|Neurexin]]		*[[Neurexin\|Neurexin]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bovin~~]]	+	[[Category: Bos taurus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Rudenko, G]]	+	[[Category: Rudenko G]]
-	[[Category: Venugopal, V]]	+	[[Category: Venugopal V]]
-	~~[[Category: Cell adhesion]]~~	+
-	~~[[Category: Synaptic adhesion molecule~~]]	+

OCA at 05:43, 15 June 2022

OCA — Wed, 15 Jun 2022 05:43:28 GMT

←Older revision		Revision as of 05:43, 15 June 2022
Line 1:		Line 1:

	==Structure of neurexin 1 alpha (domains LNS1-LNS6), with splice insert SS3==		==Structure of neurexin 1 alpha (domains LNS1-LNS6), with splice insert SS3==
-	<StructureSection load='3r05' size='340' side='right' caption='[[3r05]], [[Resolution\|resolution]] 2.95Å' scene=''>	+	<StructureSection load='3r05' size='340' side='right'caption='[[3r05]], [[Resolution\|resolution]] 2.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3r05]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R05 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3R05 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3r05]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R05 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R05 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NRXN1 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NRXN1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</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=3r05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r05 OCA], [~~http~~://pdbe.org/3r05 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3r05 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3r05 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3r05 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=3r05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r05 OCA], [https://pdbe.org/3r05 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r05 RCSB], [https://www.ebi.ac.uk/pdbsum/3r05 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r05 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/NRX1A_BOVIN NRX1A_BOVIN]] Cell surface protein involved in cell-cell-interactions, exocytosis of secretory granules and regulation of signal transmission. Function is isoform-specific. Alpha-type isoforms have a long N-terminus with six laminin G-like domains and play an important role in synaptic signal transmission. Alpha-type isoforms play a role in the regulation of calcium channel activity and Ca(2+)-triggered neurotransmitter release at synapses and at neuromuscular junctions. They play an important role in Ca(2+)-triggered exocytosis of secretory granules in pituitary gland. They may effect their functions at synapses and in endocrine cells via their interactions with proteins from the exocytotic machinery. Likewise, alpha-type isoforms play a role in regulating the activity of postsynaptic NMDA receptors, a subtype of glutamate-gated ion channels (By similarity). Both alpha-type and beta-type isoforms may play a role in the formation or maintenance of synaptic junctions via their interactions (via the extracellular domains) with neuroligin family members, CBLN1 or CBLN2. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses. Alpha-type isoforms were first identified as receptors for alpha-latrotoxin from spider venom.	+	[[https://www.uniprot.org/uniprot/NRX1A_BOVIN NRX1A_BOVIN]] Cell surface protein involved in cell-cell-interactions, exocytosis of secretory granules and regulation of signal transmission. Function is isoform-specific. Alpha-type isoforms have a long N-terminus with six laminin G-like domains and play an important role in synaptic signal transmission. Alpha-type isoforms play a role in the regulation of calcium channel activity and Ca(2+)-triggered neurotransmitter release at synapses and at neuromuscular junctions. They play an important role in Ca(2+)-triggered exocytosis of secretory granules in pituitary gland. They may effect their functions at synapses and in endocrine cells via their interactions with proteins from the exocytotic machinery. Likewise, alpha-type isoforms play a role in regulating the activity of postsynaptic NMDA receptors, a subtype of glutamate-gated ion channels (By similarity). Both alpha-type and beta-type isoforms may play a role in the formation or maintenance of synaptic junctions via their interactions (via the extracellular domains) with neuroligin family members, CBLN1 or CBLN2. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses. Alpha-type isoforms were first identified as receptors for alpha-latrotoxin from spider venom.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 3r05" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3r05" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Neurexin\|Neurexin]]
	== References ==		== References ==
	<references/>		<references/>
Line 24:		Line 27:
	</StructureSection>		</StructureSection>
	[[Category: Bovin]]		[[Category: Bovin]]
		+	[[Category: Large Structures]]
	[[Category: Rudenko, G]]		[[Category: Rudenko, G]]
	[[Category: Venugopal, V]]		[[Category: Venugopal, V]]
	[[Category: Cell adhesion]]		[[Category: Cell adhesion]]
	[[Category: Synaptic adhesion molecule]]		[[Category: Synaptic adhesion molecule]]

OCA at 09:21, 8 November 2017

OCA — Wed, 08 Nov 2017 09:21:00 GMT

←Older revision		Revision as of 09:21, 8 November 2017
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 3r05" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3r05" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Neurexin\|Neurexin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 21:32, 5 August 2016

OCA — Fri, 05 Aug 2016 21:32:52 GMT

←Older revision		Revision as of 21:32, 5 August 2016
Line 1:		Line 1:
		+
	==Structure of neurexin 1 alpha (domains LNS1-LNS6), with splice insert SS3==		==Structure of neurexin 1 alpha (domains LNS1-LNS6), with splice insert SS3==
	<StructureSection load='3r05' size='340' side='right' caption='[[3r05]], [[Resolution\|resolution]] 2.95Å' scene=''>		<StructureSection load='3r05' size='340' side='right' caption='[[3r05]], [[Resolution\|resolution]] 2.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3r05]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Bos_taurus Bos taurus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R05 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R05 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3r05]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R05 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R05 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NRXN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 ~~Bos taurus~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NRXN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</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=3r05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r05 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3r05 RCSB], [http://www.ebi.ac.uk/pdbsum/3r05 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=3r05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r05 OCA], [http://pdbe.org/3r05 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3r05 RCSB], [http://www.ebi.ac.uk/pdbsum/3r05 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3r05 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 3r05" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 24:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bos taurus~~]]	+	[[Category: Bovin]]
	[[Category: Rudenko, G]]		[[Category: Rudenko, G]]
	[[Category: Venugopal, V]]		[[Category: Venugopal, V]]
	[[Category: Cell adhesion]]		[[Category: Cell adhesion]]
	[[Category: Synaptic adhesion molecule]]		[[Category: Synaptic adhesion molecule]]

OCA at 22:05, 25 December 2014

OCA — Thu, 25 Dec 2014 22:05:04 GMT

←Older revision		Revision as of 22:05, 25 December 2014
Line 7:		Line 7:
	<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=3r05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r05 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3r05 RCSB], [http://www.ebi.ac.uk/pdbsum/3r05 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=3r05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r05 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3r05 RCSB], [http://www.ebi.ac.uk/pdbsum/3r05 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/NRX1A_BOVIN NRX1A_BOVIN]] Cell surface protein involved in cell-cell-interactions, exocytosis of secretory granules and regulation of signal transmission. Function is isoform-specific. Alpha-type isoforms have a long N-terminus with six laminin G-like domains and play an important role in synaptic signal transmission. Alpha-type isoforms play a role in the regulation of calcium channel activity and Ca(2+)-triggered neurotransmitter release at synapses and at neuromuscular junctions. They play an important role in Ca(2+)-triggered exocytosis of secretory granules in pituitary gland. They may effect their functions at synapses and in endocrine cells via their interactions with proteins from the exocytotic machinery. Likewise, alpha-type isoforms play a role in regulating the activity of postsynaptic NMDA receptors, a subtype of glutamate-gated ion channels (By similarity). Both alpha-type and beta-type isoforms may play a role in the formation or maintenance of synaptic junctions via their interactions (via the extracellular domains) with neuroligin family members, CBLN1 or CBLN2. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses. Alpha-type isoforms were first identified as receptors for alpha-latrotoxin from spider venom.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 11:30, 9 December 2014

OCA — Tue, 09 Dec 2014 11:30:36 GMT

←Older revision		Revision as of 11:30, 9 December 2014
Line 1:		Line 1:
-	[[~~Image:~~3r05.~~png~~\|~~left~~\|~~200px~~]]	+	==Structure of neurexin 1 alpha (domains LNS1-LNS6), with splice insert SS3==
		+	<StructureSection load='3r05' size='340' side='right' caption='[[3r05]], [[Resolution\|resolution]] 2.95Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3r05]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R05 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R05 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NRXN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus])</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=3r05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r05 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3r05 RCSB], [http://www.ebi.ac.uk/pdbsum/3r05 PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	alpha-Neurexins are essential synaptic adhesion molecules implicated in autism spectrum disorder and schizophrenia. The alpha-neurexin extracellular domain consists of six LNS domains interspersed by three EGF-like repeats and interacts with many different proteins in the synaptic cleft. To understand how alpha-neurexins might function as synaptic organizers, we solved the structure of the neurexin 1alpha extracellular domain (n1alpha) to 2.65 A. The L-shaped molecule can be divided into a flexible repeat I (LNS1-EGF-A-LNS2), a rigid horseshoe-shaped repeat II (LNS3-EGF-B-LNS4) with structural similarity to so-called reelin repeats, and an extended repeat III (LNS5-EGF-B-LNS6) with controlled flexibility. A 2.95 A structure of n1alpha carrying splice insert SS#3 in LNS4 reveals that SS#3 protrudes as a loop and does not alter the rigid arrangement of repeat II. The global architecture imposed by conserved structural features enables alpha-neurexins to recruit and organize proteins in distinct and variable ways, influenced by splicing, thereby promoting synaptic function.

-	~~{{STRUCTURE_3r05\| PDB=3r05 \| SCENE= }}~~	+	The structure of neurexin 1alpha reveals features promoting a role as synaptic organizer.,Chen F, Venugopal V, Murray B, Rudenko G Structure. 2011 Jun 8;19(6):779-89. Epub 2011 May 27. PMID:21620716<ref>PMID:21620716</ref>

-	~~===Structure of neurexin 1 alpha (domains LNS1-LNS6)~~, ~~with splice insert SS3===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_21620716}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3r05]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Bos_taurus Bos taurus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3R05 OCA].~~	+

	==See Also==		==See Also==
	*[[Neurexin\|Neurexin]]		*[[Neurexin\|Neurexin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:021620716<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
-	[[Category: Rudenko, G.]]	+	[[Category: Rudenko, G]]
-	[[Category: Venugopal, V.]]	+	[[Category: Venugopal, V]]
	[[Category: Cell adhesion]]		[[Category: Cell adhesion]]
	[[Category: Synaptic adhesion molecule]]		[[Category: Synaptic adhesion molecule]]

OCA at 22:11, 20 October 2012

OCA — Sat, 20 Oct 2012 22:11:58 GMT

←Older revision		Revision as of 22:11, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3r05]] is a 2 chain structure ~~of [[Neurexin]]~~ with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R05 OCA].	+	[[3r05]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R05 OCA].

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

OCA at 15:32, 27 July 2012

OCA — Fri, 27 Jul 2012 15:32:40 GMT

←Older revision		Revision as of 15:32, 27 July 2012
Line 1:		Line 1:
-	[[Image:3r05.~~jpg~~\|left\|200px]]	+	[[Image:3r05.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3r05", 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_3r05\| PDB=3r05 \| SCENE= }}		{{STRUCTURE_3r05\| PDB=3r05 \| SCENE= }}

	===Structure of neurexin 1 alpha (domains LNS1-LNS6), with splice insert SS3===		===Structure of neurexin 1 alpha (domains LNS1-LNS6), with splice insert SS3===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_21620716}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 21620716 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_21620716}}		{{ABSTRACT_PUBMED_21620716}}

	==About this Structure==		==About this Structure==
-	[[3r05]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R05 OCA].	+	[[3r05]] is a 2 chain structure of [[Neurexin]] with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R05 OCA].
		+
		+	==See Also==
		+	*[[Neurexin\|Neurexin]]

	==Reference==		==Reference==

OCA at 06:21, 15 June 2011

OCA — Wed, 15 Jun 2011 06:21:34 GMT

←Older revision		Revision as of 06:21, 15 June 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3r05.jpg\|left\|200px]]

-	The ~~entry 3r05~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3r05", 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_3r05\| PDB=3r05 \| SCENE= }}

-	~~Authors: Venugopal~~, ~~V., Rudenko, G.~~	+	===Structure of neurexin 1 alpha (domains LNS1-LNS6), with splice insert SS3===

-	~~Description~~:	+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_21620716}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 21620716 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_21620716}}
		+
		+	==About this Structure==
		+	[[3r05]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R05 OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:021620716</ref><references group="xtra"/>
		+	[[Category: Bos taurus]]
		+	[[Category: Rudenko, G.]]
		+	[[Category: Venugopal, V.]]
		+	[[Category: Cell adhesion]]
		+	[[Category: Synaptic adhesion molecule]]

OCA at 04:18, 12 May 2011

OCA — Thu, 12 May 2011 04:18:43 GMT

←Older revision		Revision as of 04:18, 12 May 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3r05 is ON HOLD	+	The entry 3r05 is ON HOLD until Paper Publication

	Authors: Venugopal, V., Rudenko, G.		Authors: Venugopal, V., Rudenko, G.

	Description:		Description: