3asi - Revision history

OCA at 15:53, 4 October 2023

OCA — Wed, 04 Oct 2023 15:53:59 GMT

←Older revision		Revision as of 15:53, 4 October 2023
Line 3:		Line 3:
	<StructureSection load='3asi' size='340' side='right'caption='[[3asi]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='3asi' size='340' side='right'caption='[[3asi]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3asi]] is a 1 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=3ASI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ASI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3asi]] is a 1 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=3ASI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ASI FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>~~, ~~<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]] 2.3Å</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=CA:CALCIUM+ION'>CA</scene>, <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=3asi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3asi OCA], [https://pdbe.org/3asi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3asi RCSB], [https://www.ebi.ac.uk/pdbsum/3asi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3asi 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=3asi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3asi OCA], [https://pdbe.org/3asi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3asi RCSB], [https://www.ebi.ac.uk/pdbsum/3asi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3asi 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;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bovin~~]]	+	[[Category: Bos taurus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Nogi, T]]	+	[[Category: Nogi T]]
-	[[Category: Takagi, J]]	+	[[Category: Takagi J]]
-	[[Category: Tanaka, H]]	+	[[Category: Tanaka H]]
-	[[Category: Yasui, N]]	+	[[Category: Yasui N]]
-	~~[[Category: Beta-sandwich]]~~	+
-	~~[[Category: Cell adhesion]]~~	+
-	~~[[Category: Membrane]]~~	+
-	~~[[Category: N-glycosylation]]~~	+
-	~~[[Category: Neuroligin]]~~	+
-	~~[[Category: Synapse maturation~~]]	+

OCA at 15:03, 29 December 2021

OCA — Wed, 29 Dec 2021 15:03:09 GMT

←Older revision		Revision as of 15:03, 29 December 2021
Line 1:		Line 1:

	==Alpha-Neurexin-1 ectodomain fragment; LNS5-EGF3-LNS6==		==Alpha-Neurexin-1 ectodomain fragment; LNS5-EGF3-LNS6==
-	<StructureSection load='3asi' size='340' side='right' caption='[[3asi]], [[Resolution\|resolution]] 2.30Å' scene=''>	+	<StructureSection load='3asi' size='340' side='right'caption='[[3asi]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3asi]] is a 1 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=3ASI OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3ASI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3asi]] is a 1 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=3ASI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ASI FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <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=CA:CALCIUM+ION'>CA</scene>, <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=3asi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3asi OCA], [~~http~~://pdbe.org/3asi PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3asi RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3asi PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3asi 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=3asi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3asi OCA], [https://pdbe.org/3asi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3asi RCSB], [https://www.ebi.ac.uk/pdbsum/3asi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3asi 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 27:		Line 27:
	</StructureSection>		</StructureSection>
	[[Category: Bovin]]		[[Category: Bovin]]
		+	[[Category: Large Structures]]
	[[Category: Nogi, T]]		[[Category: Nogi, T]]
	[[Category: Takagi, J]]		[[Category: Takagi, J]]

OCA at 03:49, 5 August 2016

OCA — Fri, 05 Aug 2016 03:49:49 GMT

←Older revision		Revision as of 03:49, 5 August 2016
Line 1:		Line 1:
		+
	==Alpha-Neurexin-1 ectodomain fragment; LNS5-EGF3-LNS6==		==Alpha-Neurexin-1 ectodomain fragment; LNS5-EGF3-LNS6==
	<StructureSection load='3asi' size='340' side='right' caption='[[3asi]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='3asi' size='340' side='right' caption='[[3asi]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3asi]] is a 1 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=3ASI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ASI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3asi]] is a 1 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=3ASI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ASI FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <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=CA:CALCIUM+ION'>CA</scene>, <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=3asi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3asi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3asi RCSB], [http://www.ebi.ac.uk/pdbsum/3asi 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=3asi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3asi OCA], [http://pdbe.org/3asi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3asi RCSB], [http://www.ebi.ac.uk/pdbsum/3asi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3asi 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 3asi" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 24:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bos taurus~~]]	+	[[Category: Bovin]]
	[[Category: Nogi, T]]		[[Category: Nogi, T]]
	[[Category: Takagi, J]]		[[Category: Takagi, J]]

OCA at 15:36, 25 December 2014

OCA — Thu, 25 Dec 2014 15:36:49 GMT

←Older revision		Revision as of 15:36, 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=3asi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3asi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3asi RCSB], [http://www.ebi.ac.uk/pdbsum/3asi 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=3asi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3asi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3asi RCSB], [http://www.ebi.ac.uk/pdbsum/3asi 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 ==
Line 23:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
-	[[Category: Nogi, T.]]	+	[[Category: Nogi, T]]
-	[[Category: Takagi, J.]]	+	[[Category: Takagi, J]]
-	[[Category: Tanaka, H.]]	+	[[Category: Tanaka, H]]
-	[[Category: Yasui, N.]]	+	[[Category: Yasui, N]]
	[[Category: Beta-sandwich]]		[[Category: Beta-sandwich]]
	[[Category: Cell adhesion]]		[[Category: Cell adhesion]]

OCA at 09:32, 5 November 2014

OCA — Wed, 05 Nov 2014 09:32:41 GMT

←Older revision		Revision as of 09:32, 5 November 2014
Line 1:		Line 1:
-	[[~~Image:~~3asi.~~png~~\|~~left~~\|~~200px~~]]	+	==Alpha-Neurexin-1 ectodomain fragment; LNS5-EGF3-LNS6==
		+	<StructureSection load='3asi' size='340' side='right' caption='[[3asi]], [[Resolution\|resolution]] 2.30Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3asi]] is a 1 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=3ASI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ASI FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <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=3asi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3asi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3asi RCSB], [http://www.ebi.ac.uk/pdbsum/3asi PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Neurexins (Nrxs) are presynaptic membrane proteins with a single membrane-spanning domain that mediate asymmetric trans-synaptic cell adhesion by binding to their postsynaptic receptor neuroligins. alpha-Nrx has a large extracellular region comprised of multiple copies of laminin, neurexin, sex-hormone-binding globulin (LNS) domains and epidermal growth factor (EGF) modules, while that of beta-Nrx has but a single LNS domain. It has long been known that the larger alpha-Nrx and the shorter beta-Nrx show distinct binding behaviors toward different isoforms/variants of neuroligins, although the underlying mechanism has yet to be elucidated. Here, we describe the crystal structure of a fragment corresponding to the C-terminal one-third of the Nrx1alpha ectodomain, consisting of LNS5-EGF3-LNS6. The 2.3 A-resolution structure revealed the presence of a domain configuration that was rigidified by inter-domain contacts, as opposed to the more common flexible "beads-on-a-string" arrangement. Although the neuroligin-binding site on the LNS6 domain was completely exposed, the location of the alpha-Nrx specific LNS5-EGF3 segment proved incompatible with the loop segment inserted in the B+ neuroligin variant, which explains the variant-specific neuroligin recognition capability observed in alpha-Nrx. This, combined with a low-resolution molecular envelope obtained by a single particle reconstruction performed on negatively stained full-length Nrx1alpha sample, allowed us to derive a structural model of the alpha-Nrx ectodomain. This model will help us understand not only how the large alpha-Nrx ectodomain is accommodated in the synaptic cleft, but also how the trans-synaptic adhesion mediated by alpha- and beta-Nrxs could differentially affect synaptic structure and function.

-	~~{{STRUCTURE_3asi\| PDB=3asi \| SCENE= }}~~	+	Structural Basis for Variant-Specific Neuroligin-Binding by alpha-Neurexin.,Tanaka H, Nogi T, Yasui N, Iwasaki K, Takagi J PLoS One. 2011 Apr 28;6(4):e19411. PMID:21552542<ref>PMID:21552542</ref>

-	~~===Alpha-Neurexin-1 ectodomain fragment~~; ~~LNS5-EGF3-LNS6===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_21552542}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3asi]] is~~ a ~~1 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=3ASI OCA].~~	+

	==See Also==		==See Also==
	*[[Neurexin\|Neurexin]]		*[[Neurexin\|Neurexin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:021552542<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
	[[Category: Nogi, T.]]		[[Category: Nogi, T.]]

OCA at 18:25, 20 October 2012

OCA — Sat, 20 Oct 2012 18:25:40 GMT

←Older revision		Revision as of 18:25, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3asi]] is a 1 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=3ASI OCA].	+	[[3asi]] is a 1 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=3ASI OCA].

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

OCA at 04:02, 27 July 2012

OCA — Fri, 27 Jul 2012 04:02:45 GMT

←Older revision		Revision as of 04:02, 27 July 2012
Line 1:		Line 1:
	[[Image:3asi.png\|left\|200px]]		[[Image:3asi.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3asi", 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_3asi\| PDB=3asi \| SCENE= }}		{{STRUCTURE_3asi\| PDB=3asi \| SCENE= }}

	===Alpha-Neurexin-1 ectodomain fragment; LNS5-EGF3-LNS6===		===Alpha-Neurexin-1 ectodomain fragment; LNS5-EGF3-LNS6===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_21552542}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 21552542 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_21552542}}		{{ABSTRACT_PUBMED_21552542}}

	==About this Structure==		==About this Structure==
-	[[3asi]] is a 1 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=3ASI OCA].	+	[[3asi]] is a 1 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=3ASI OCA].
		+
		+	==See Also==
		+	*[[Neurexin\|Neurexin]]

	==Reference==		==Reference==
Line 28:		Line 20:
	[[Category: Tanaka, H.]]		[[Category: Tanaka, H.]]
	[[Category: Yasui, N.]]		[[Category: Yasui, N.]]
		+	[[Category: Beta-sandwich]]
		+	[[Category: Cell adhesion]]
		+	[[Category: Membrane]]
		+	[[Category: N-glycosylation]]
		+	[[Category: Neuroligin]]
		+	[[Category: Synapse maturation]]

OCA at 05:06, 1 June 2011

OCA — Wed, 01 Jun 2011 05:06:59 GMT

←Older revision		Revision as of 05:06, 1 June 2011
Line 1:		Line 1:
-	[[Image:3asi.~~jpg~~\|left\|200px]]	+	[[Image:3asi.png\|left\|200px]]

	<!--		<!--
Line 11:		Line 11:
	===Alpha-Neurexin-1 ectodomain fragment; LNS5-EGF3-LNS6===		===Alpha-Neurexin-1 ectodomain fragment; LNS5-EGF3-LNS6===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_21552542}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 21552542 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_21552542}}

	==About this Structure==		==About this Structure==
	[[3asi]] is a 1 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=3ASI OCA].		[[3asi]] is a 1 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=3ASI OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:021552542</ref><references group="xtra"/>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
	[[Category: Nogi, T.]]		[[Category: Nogi, T.]]

OCA at 05:21, 13 April 2011

OCA — Wed, 13 Apr 2011 05:21:57 GMT

←Older revision		Revision as of 05:21, 13 April 2011
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-	~~'''Unreleased structure'''~~	+	[[Image:3asi.jpg\|left\|200px]]

-	The ~~entry 3asi~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3asi", 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_3asi\| PDB=3asi \| SCENE= }}

-	~~Authors: Tanaka, H., Nogi, T., Yasui, N., Takagi, J.~~	+	===Alpha-Neurexin-1 ectodomain fragment; LNS5-EGF3-LNS6===

-	~~Description~~: ~~Synaptic adhesion molecule~~	+
		+	==About this Structure==
		+	[[3asi]] is a 1 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=3ASI OCA].
		+	[[Category: Bos taurus]]
		+	[[Category: Nogi, T.]]
		+	[[Category: Takagi, J.]]
		+	[[Category: Tanaka, H.]]
		+	[[Category: Yasui, N.]]

OCA at 06:30, 2 March 2011

OCA — Wed, 02 Mar 2011 06:30:51 GMT

←Older revision		Revision as of 06:30, 2 March 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Tanaka, H., Nogi, T., Yasui, N., Takagi, J.		Authors: Tanaka, H., Nogi, T., Yasui, N., Takagi, J.

	Description: Synaptic adhesion molecule		Description: Synaptic adhesion molecule