5h48 - Revision history

OCA at 07:23, 9 August 2023

OCA — Wed, 09 Aug 2023 07:23:17 GMT

←Older revision		Revision as of 07:23, 9 August 2023
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	<StructureSection load='5h48' size='340' side='right'caption='[[5h48]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='5h48' size='340' side='right'caption='[[5h48]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5h48]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H48 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5H48 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5h48]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H48 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H48 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]] 2.2Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">~~[[5h49\|5h49]], [[5h4b\|5h4b]], [[5h4c\|5h4c]]~~</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'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5h48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h48 OCA], [~~http~~://pdbe.org/5h48 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5h48 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5h48 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5h48 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=5h48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h48 OCA], [https://pdbe.org/5h48 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h48 RCSB], [https://www.ebi.ac.uk/pdbsum/5h48 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h48 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/CBLN1_RAT CBLN1_RAT]] Required for synapse integrity and synaptic plasticity. During cerebellar synapse formation, essential for the formation and maintenance of parallel fiber and Purkinje cell synapses. When parallel fibers make contact with Purkinje spines, CBLN1 interaction with GRID2 triggers the recruitment of NRXN1 and secretory vesicles to the sites of contact. NRXN1-CBLN1-GRID2 signaling induces presynaptic morphological changes, which may further accumulate pre- and postsynaptic components to promote bidirectional maturation of parallel fiber - Purkinje cell functionally active synapses by a positive feedback mechanism. Required for CBLN3 export from the endoplasmic reticulum and secretion (By similarity). The cerebellin exerts neuromodulatory functions. Directly stimulates norepinephrine release via the adenylate cyclase/PKA-dependent signaling pathway; and indirectly enhances adrenocortical secretion in vivo, through a paracrine mechanism involving medullary catecholamine release. A conversion to [des-Ser1]-cerebellin by endopeptidases seems to be required for its autocrine-paracrine regulatory functions.<ref>PMID:10688962</ref> <ref>PMID:15702230</ref>	+	[https://www.uniprot.org/uniprot/CBLN1_RAT CBLN1_RAT] Required for synapse integrity and synaptic plasticity. During cerebellar synapse formation, essential for the formation and maintenance of parallel fiber and Purkinje cell synapses. When parallel fibers make contact with Purkinje spines, CBLN1 interaction with GRID2 triggers the recruitment of NRXN1 and secretory vesicles to the sites of contact. NRXN1-CBLN1-GRID2 signaling induces presynaptic morphological changes, which may further accumulate pre- and postsynaptic components to promote bidirectional maturation of parallel fiber - Purkinje cell functionally active synapses by a positive feedback mechanism. Required for CBLN3 export from the endoplasmic reticulum and secretion (By similarity). The cerebellin exerts neuromodulatory functions. Directly stimulates norepinephrine release via the adenylate cyclase/PKA-dependent signaling pathway; and indirectly enhances adrenocortical secretion in vivo, through a paracrine mechanism involving medullary catecholamine release. A conversion to [des-Ser1]-cerebellin by endopeptidases seems to be required for its autocrine-paracrine regulatory functions.<ref>PMID:10688962</ref> <ref>PMID:15702230</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Ding, J]]	+	[[Category: Rattus norvegicus]]
-	[[Category: Shen, J]]	+	[[Category: Ding J]]
-	[[Category: Zhang, H]]	+	[[Category: Shen J]]
-	[[Category: Zhong, C]]	+	[[Category: Zhang H]]
-	~~[[Category: C1q domain]]~~	+	[[Category: Zhong C]]
-	~~[[Category: C1q/tnf superfamily]]~~	+
-	~~[[Category: Protein binding]]~~	+
-	~~[[Category: Receptor specificity]]~~	+
-	~~[[Category: Synaptogenesis~~]]	+

OCA at 06:52, 20 May 2020

OCA — Wed, 20 May 2020 06:52:06 GMT

←Older revision		Revision as of 06:52, 20 May 2020
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	==Crystal structure of Cbln1==		==Crystal structure of Cbln1==
-	<StructureSection load='5h48' size='340' side='right' caption='[[5h48]], [[Resolution\|resolution]] 2.20Å' scene=''>	+	<StructureSection load='5h48' size='340' side='right'caption='[[5h48]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5h48]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H48 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5H48 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5h48]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H48 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5H48 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='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5h49\|5h49]], [[5h4b\|5h4b]], [[5h4c\|5h4c]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5h49\|5h49]], [[5h4b\|5h4b]], [[5h4c\|5h4c]]</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=5h48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h48 OCA], [http://pdbe.org/5h48 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h48 RCSB], [http://www.ebi.ac.uk/pdbsum/5h48 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h48 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=5h48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h48 OCA], [http://pdbe.org/5h48 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h48 RCSB], [http://www.ebi.ac.uk/pdbsum/5h48 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h48 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 23:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Ding, J]]		[[Category: Ding, J]]
	[[Category: Shen, J]]		[[Category: Shen, J]]

OCA at 04:28, 21 September 2017

OCA — Thu, 21 Sep 2017 04:28:43 GMT

←Older revision		Revision as of 04:28, 21 September 2017
Line 10:		Line 10:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/CBLN1_RAT CBLN1_RAT]] Required for synapse integrity and synaptic plasticity. During cerebellar synapse formation, essential for the formation and maintenance of parallel fiber and Purkinje cell synapses. When parallel fibers make contact with Purkinje spines, CBLN1 interaction with GRID2 triggers the recruitment of NRXN1 and secretory vesicles to the sites of contact. NRXN1-CBLN1-GRID2 signaling induces presynaptic morphological changes, which may further accumulate pre- and postsynaptic components to promote bidirectional maturation of parallel fiber - Purkinje cell functionally active synapses by a positive feedback mechanism. Required for CBLN3 export from the endoplasmic reticulum and secretion (By similarity). The cerebellin exerts neuromodulatory functions. Directly stimulates norepinephrine release via the adenylate cyclase/PKA-dependent signaling pathway; and indirectly enhances adrenocortical secretion in vivo, through a paracrine mechanism involving medullary catecholamine release. A conversion to [des-Ser1]-cerebellin by endopeptidases seems to be required for its autocrine-paracrine regulatory functions.<ref>PMID:10688962</ref> <ref>PMID:15702230</ref>		[[http://www.uniprot.org/uniprot/CBLN1_RAT CBLN1_RAT]] Required for synapse integrity and synaptic plasticity. During cerebellar synapse formation, essential for the formation and maintenance of parallel fiber and Purkinje cell synapses. When parallel fibers make contact with Purkinje spines, CBLN1 interaction with GRID2 triggers the recruitment of NRXN1 and secretory vesicles to the sites of contact. NRXN1-CBLN1-GRID2 signaling induces presynaptic morphological changes, which may further accumulate pre- and postsynaptic components to promote bidirectional maturation of parallel fiber - Purkinje cell functionally active synapses by a positive feedback mechanism. Required for CBLN3 export from the endoplasmic reticulum and secretion (By similarity). The cerebellin exerts neuromodulatory functions. Directly stimulates norepinephrine release via the adenylate cyclase/PKA-dependent signaling pathway; and indirectly enhances adrenocortical secretion in vivo, through a paracrine mechanism involving medullary catecholamine release. A conversion to [des-Ser1]-cerebellin by endopeptidases seems to be required for its autocrine-paracrine regulatory functions.<ref>PMID:10688962</ref> <ref>PMID:15702230</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Unlike cerebellin 1 (Cbln1), which bridges neurexin (Nrxn) receptors and delta-type glutamate receptors in a trans-synaptic triad, Cbln4 was reported to have no or weak binding for the receptors despite sharing approximately 70% sequence identity with Cbln1. Here, we report crystal structures of the homotrimers of the C1q domain of Cbln1 and Cbln4 at 2.2 and 2.3 A resolution, respectively. Comparison of the structures suggests that the difference between Cbln1 and Cbln4 in GluD2 binding might be because of their sequence and structural divergence in loop CD. Surprisingly, we show that Cbln4 binds to Nrxn1beta and forms a stable complex with the laminin, nectin, sex-hormone binding globulin (LNS) domain of Nrxn1beta. Furthermore, the negative-stain electron microscopy reconstruction of hexameric full-length Cbln1 at 13 A resolution and that of the Cbln4/Nrxn1beta complex at 19 A resolution suggest that Nrxn1beta binds to the N-terminal region of Cbln4, probably through strand beta10 of the S4 insert.
		+
		+	Cbln1 and Cbln4 Are Structurally Similar but Differ in GluD2 Binding Interactions.,Zhong C, Shen J, Zhang H, Li G, Shen S, Wang F, Hu K, Cao L, He Y, Ding J Cell Rep. 2017 Sep 5;20(10):2328-2340. doi: 10.1016/j.celrep.2017.08.031. PMID:28877468<ref>PMID:28877468</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5h48" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:41, 13 September 2017

OCA — Wed, 13 Sep 2017 09:41:25 GMT

←Older revision		Revision as of 09:41, 13 September 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5h48 is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Crystal structure of Cbln1==
-		+	<StructureSection load='5h48' size='340' side='right' caption='[[5h48]], [[Resolution\|resolution]] 2.20Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5h48]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H48 FirstGlance]. <br>
-	~~Description~~:	+	</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>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5h49\|5h49]], [[5h4b\|5h4b]], [[5h4c\|5h4c]]</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=5h48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h48 OCA], [http://pdbe.org/5h48 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h48 RCSB], [http://www.ebi.ac.uk/pdbsum/5h48 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h48 ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CBLN1_RAT CBLN1_RAT]] Required for synapse integrity and synaptic plasticity. During cerebellar synapse formation, essential for the formation and maintenance of parallel fiber and Purkinje cell synapses. When parallel fibers make contact with Purkinje spines, CBLN1 interaction with GRID2 triggers the recruitment of NRXN1 and secretory vesicles to the sites of contact. NRXN1-CBLN1-GRID2 signaling induces presynaptic morphological changes, which may further accumulate pre- and postsynaptic components to promote bidirectional maturation of parallel fiber - Purkinje cell functionally active synapses by a positive feedback mechanism. Required for CBLN3 export from the endoplasmic reticulum and secretion (By similarity). The cerebellin exerts neuromodulatory functions. Directly stimulates norepinephrine release via the adenylate cyclase/PKA-dependent signaling pathway; and indirectly enhances adrenocortical secretion in vivo, through a paracrine mechanism involving medullary catecholamine release. A conversion to [des-Ser1]-cerebellin by endopeptidases seems to be required for its autocrine-paracrine regulatory functions.<ref>PMID:10688962</ref> <ref>PMID:15702230</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Ding, J]]
		+	[[Category: Shen, J]]
		+	[[Category: Zhang, H]]
		+	[[Category: Zhong, C]]
		+	[[Category: C1q domain]]
		+	[[Category: C1q/tnf superfamily]]
		+	[[Category: Protein binding]]
		+	[[Category: Receptor specificity]]
		+	[[Category: Synaptogenesis]]

OCA at 07:39, 5 April 2017

OCA — Wed, 05 Apr 2017 07:39:04 GMT

←Older revision		Revision as of 07:39, 5 April 2017
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5h48 is ON HOLD	+	The entry 5h48 is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "5h48" [edit=sysop:move=sysop]

OCA — Fri, 09 Dec 2016 13:43:04 GMT

Protected "5h48" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:43, 9 December 2016

OCA: New page: '''Unreleased structure''' The entry 5h48 is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Fri, 09 Dec 2016 13:43:03 GMT

New page: '''Unreleased structure''' The entry 5h48 is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5h48 is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]