1pxu - Revision history

OCA at 09:52, 16 August 2023

OCA — Wed, 16 Aug 2023 09:52:21 GMT

←Older revision		Revision as of 09:52, 16 August 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1pxu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PXU FirstGlance]. <br>		<table><tr><td colspan='2'>[[1pxu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PXU 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=1pxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pxu OCA], [https://pdbe.org/1pxu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pxu RCSB], [https://www.ebi.ac.uk/pdbsum/1pxu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pxu ProSAT]</span></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pxu OCA], [https://pdbe.org/1pxu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pxu RCSB], [https://www.ebi.ac.uk/pdbsum/1pxu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pxu ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 11:49, 14 June 2023

OCA — Wed, 14 Jun 2023 11:49:13 GMT

←Older revision		Revision as of 11:49, 14 June 2023
Line 3:		Line 3:
	<StructureSection load='1pxu' size='340' side='right'caption='[[1pxu]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='1pxu' size='340' side='right'caption='[[1pxu]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1pxu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Chick Chick~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PXU FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1pxu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PXU FirstGlance]. <br>
-	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jb3\|1jb3]], [[1jc7\|1jc7]]</div></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=1pxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pxu OCA], [https://pdbe.org/1pxu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pxu RCSB], [https://www.ebi.ac.uk/pdbsum/1pxu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pxu 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=1pxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pxu OCA], [https://pdbe.org/1pxu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pxu RCSB], [https://www.ebi.ac.uk/pdbsum/1pxu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pxu ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/AGRIN_CHICK AGRIN_CHICK]] Isoform 1: heparan sulfate basal lamina glycoprotein that plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ) and directs key events in postsynaptic differentiation. Component of the AGRN-LRP4 receptor complex that induces the phosphorylation and activation of MUSK. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Calcium ions are required for maximal AChR clustering. AGRN funtion in neurons is highly regulated by alternative splicing, glycan binding and proteolytic processing. Modulates calcium ion homestasis in neurons, specifically by inducing an increase in cytoplasmic calcium ions. Functions differentially in the central nervous system (CNS) by inhibiting the alpha(3)-subtype of Na+/K+-ATPase and evoking depolarization at CNS synapses.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref> Isoform 9: transmembrane agrin (TM-agrin), the predominant form in neurons of the brain, induces dendritic filopodia and synapse formation in mature hippocampal neurons in large part due to the attached glycosaminoglycan chains and the action of Rho-family GTPases.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref> Isoform 2, isoform 4 and isoform 7: muscle agrin isoforms, which lack the 8-amino acid insert at the 'B' site, but with the insert at the'A' site have no AChr clustering activity nor MUSK activation but bind heparin. Bind alpha-dystroglycan with lower affinity.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref> Isoform 5: muscle agrin A0B0 lacking inserts at both 'A' and 'B' sites has no heparin-binding nor AChR clustering activity but binds strongly alpha-dystroglycan.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref> Agrin N-terminal 110 kDa subunit: is involved in modulation of growth factor signaling (By similarity). Involved also in the regulation of neurite outgrowth probably due to the presence of the glycosaminoglcan (GAG) side chains of heparan and chondroitin sulfate attached to the Ser/Thr- and Gly/Ser-rich regions. Also involved in modulation of growth factor signaling.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref> Agrin C-terminal 22 kDa fragment: this released fragment is important for agrin signaling and to exert a maximal dendritic filopodia-inducing effect. All 'B' splice variants of this fragment also show an increase in the number of filopodia.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref>	+	[https://www.uniprot.org/uniprot/AGRIN_CHICK AGRIN_CHICK] Isoform 1: heparan sulfate basal lamina glycoprotein that plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ) and directs key events in postsynaptic differentiation. Component of the AGRN-LRP4 receptor complex that induces the phosphorylation and activation of MUSK. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Calcium ions are required for maximal AChR clustering. AGRN funtion in neurons is highly regulated by alternative splicing, glycan binding and proteolytic processing. Modulates calcium ion homestasis in neurons, specifically by inducing an increase in cytoplasmic calcium ions. Functions differentially in the central nervous system (CNS) by inhibiting the alpha(3)-subtype of Na+/K+-ATPase and evoking depolarization at CNS synapses.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref> Isoform 9: transmembrane agrin (TM-agrin), the predominant form in neurons of the brain, induces dendritic filopodia and synapse formation in mature hippocampal neurons in large part due to the attached glycosaminoglycan chains and the action of Rho-family GTPases.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref> Isoform 2, isoform 4 and isoform 7: muscle agrin isoforms, which lack the 8-amino acid insert at the 'B' site, but with the insert at the'A' site have no AChr clustering activity nor MUSK activation but bind heparin. Bind alpha-dystroglycan with lower affinity.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref> Isoform 5: muscle agrin A0B0 lacking inserts at both 'A' and 'B' sites has no heparin-binding nor AChR clustering activity but binds strongly alpha-dystroglycan.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref> Agrin N-terminal 110 kDa subunit: is involved in modulation of growth factor signaling (By similarity). Involved also in the regulation of neurite outgrowth probably due to the presence of the glycosaminoglcan (GAG) side chains of heparan and chondroitin sulfate attached to the Ser/Thr- and Gly/Ser-rich regions. Also involved in modulation of growth factor signaling.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref> Agrin C-terminal 22 kDa fragment: this released fragment is important for agrin signaling and to exert a maximal dendritic filopodia-inducing effect. All 'B' splice variants of this fragment also show an increase in the number of filopodia.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Chick~~]]	+	[[Category: Gallus gallus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Stetefeld, J]]	+	[[Category: Stetefeld J]]
-	~~[[Category: Agrin]]~~	+
-	~~[[Category: Structural protein~~]]	+

OCA at 09:36, 8 September 2021

OCA — Wed, 08 Sep 2021 09:36:09 GMT

←Older revision		Revision as of 09:36, 8 September 2021
Line 3:		Line 3:
	<StructureSection load='1pxu' size='340' side='right'caption='[[1pxu]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='1pxu' size='340' side='right'caption='[[1pxu]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1pxu]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXU OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1PXU FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1pxu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PXU FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1jb3\|1jb3]], [[1jc7\|1jc7]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jb3\|1jb3]], [[1jc7\|1jc7]]</div></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=1pxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pxu OCA], [~~http~~://pdbe.org/1pxu PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1pxu RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1pxu PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1pxu 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=1pxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pxu OCA], [https://pdbe.org/1pxu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pxu RCSB], [https://www.ebi.ac.uk/pdbsum/1pxu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pxu ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/AGRIN_CHICK AGRIN_CHICK]] Isoform 1: heparan sulfate basal lamina glycoprotein that plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ) and directs key events in postsynaptic differentiation. Component of the AGRN-LRP4 receptor complex that induces the phosphorylation and activation of MUSK. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Calcium ions are required for maximal AChR clustering. AGRN funtion in neurons is highly regulated by alternative splicing, glycan binding and proteolytic processing. Modulates calcium ion homestasis in neurons, specifically by inducing an increase in cytoplasmic calcium ions. Functions differentially in the central nervous system (CNS) by inhibiting the alpha(3)-subtype of Na+/K+-ATPase and evoking depolarization at CNS synapses.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref> Isoform 9: transmembrane agrin (TM-agrin), the predominant form in neurons of the brain, induces dendritic filopodia and synapse formation in mature hippocampal neurons in large part due to the attached glycosaminoglycan chains and the action of Rho-family GTPases.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref> Isoform 2, isoform 4 and isoform 7: muscle agrin isoforms, which lack the 8-amino acid insert at the 'B' site, but with the insert at the'A' site have no AChr clustering activity nor MUSK activation but bind heparin. Bind alpha-dystroglycan with lower affinity.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref> Isoform 5: muscle agrin A0B0 lacking inserts at both 'A' and 'B' sites has no heparin-binding nor AChR clustering activity but binds strongly alpha-dystroglycan.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref> Agrin N-terminal 110 kDa subunit: is involved in modulation of growth factor signaling (By similarity). Involved also in the regulation of neurite outgrowth probably due to the presence of the glycosaminoglcan (GAG) side chains of heparan and chondroitin sulfate attached to the Ser/Thr- and Gly/Ser-rich regions. Also involved in modulation of growth factor signaling.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref> Agrin C-terminal 22 kDa fragment: this released fragment is important for agrin signaling and to exert a maximal dendritic filopodia-inducing effect. All 'B' splice variants of this fragment also show an increase in the number of filopodia.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref>	+	[[https://www.uniprot.org/uniprot/AGRIN_CHICK AGRIN_CHICK]] Isoform 1: heparan sulfate basal lamina glycoprotein that plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ) and directs key events in postsynaptic differentiation. Component of the AGRN-LRP4 receptor complex that induces the phosphorylation and activation of MUSK. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Calcium ions are required for maximal AChR clustering. AGRN funtion in neurons is highly regulated by alternative splicing, glycan binding and proteolytic processing. Modulates calcium ion homestasis in neurons, specifically by inducing an increase in cytoplasmic calcium ions. Functions differentially in the central nervous system (CNS) by inhibiting the alpha(3)-subtype of Na+/K+-ATPase and evoking depolarization at CNS synapses.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref> Isoform 9: transmembrane agrin (TM-agrin), the predominant form in neurons of the brain, induces dendritic filopodia and synapse formation in mature hippocampal neurons in large part due to the attached glycosaminoglycan chains and the action of Rho-family GTPases.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref> Isoform 2, isoform 4 and isoform 7: muscle agrin isoforms, which lack the 8-amino acid insert at the 'B' site, but with the insert at the'A' site have no AChr clustering activity nor MUSK activation but bind heparin. Bind alpha-dystroglycan with lower affinity.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref> Isoform 5: muscle agrin A0B0 lacking inserts at both 'A' and 'B' sites has no heparin-binding nor AChR clustering activity but binds strongly alpha-dystroglycan.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref> Agrin N-terminal 110 kDa subunit: is involved in modulation of growth factor signaling (By similarity). Involved also in the regulation of neurite outgrowth probably due to the presence of the glycosaminoglcan (GAG) side chains of heparan and chondroitin sulfate attached to the Ser/Thr- and Gly/Ser-rich regions. Also involved in modulation of growth factor signaling.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref> Agrin C-terminal 22 kDa fragment: this released fragment is important for agrin signaling and to exert a maximal dendritic filopodia-inducing effect. All 'B' splice variants of this fragment also show an increase in the number of filopodia.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 10:16, 27 November 2019

OCA — Wed, 27 Nov 2019 10:16:14 GMT

←Older revision		Revision as of 10:16, 27 November 2019
Line 1:		Line 1:

	==Crystal structure of chicken NtA from a eukaryotic source at 2.2A resolution==		==Crystal structure of chicken NtA from a eukaryotic source at 2.2A resolution==
-	<StructureSection load='1pxu' size='340' side='right' caption='[[1pxu]], [[Resolution\|resolution]] 2.20Å' scene=''>	+	<StructureSection load='1pxu' size='340' side='right'caption='[[1pxu]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1pxu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PXU FirstGlance]. <br>		<table><tr><td colspan='2'>[[1pxu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PXU FirstGlance]. <br>
Line 18:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 1pxu" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1pxu" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Agrin 3D structures\|Agrin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 23:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Chick]]		[[Category: Chick]]
		+	[[Category: Large Structures]]
	[[Category: Stetefeld, J]]		[[Category: Stetefeld, J]]
	[[Category: Agrin]]		[[Category: Agrin]]
	[[Category: Structural protein]]		[[Category: Structural protein]]

OCA at 08:15, 24 February 2018

OCA — Sat, 24 Feb 2018 08:15:52 GMT

←Older revision		Revision as of 08:15, 24 February 2018
Line 1:		Line 1:
		+
	==Crystal structure of chicken NtA from a eukaryotic source at 2.2A resolution==		==Crystal structure of chicken NtA from a eukaryotic source at 2.2A resolution==
	<StructureSection load='1pxu' size='340' side='right' caption='[[1pxu]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='1pxu' size='340' side='right' caption='[[1pxu]], [[Resolution\|resolution]] 2.20Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1pxu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PXU FirstGlance]. <br>		<table><tr><td colspan='2'>[[1pxu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PXU FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1jb3\|1jb3]], [[1jc7\|1jc7]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1jb3\|1jb3]], [[1jc7\|1jc7]]</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=1pxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pxu OCA], [http://pdbe.org/1pxu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pxu RCSB], [http://www.ebi.ac.uk/pdbsum/1pxu 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=1pxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pxu OCA], [http://pdbe.org/1pxu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pxu RCSB], [http://www.ebi.ac.uk/pdbsum/1pxu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pxu ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 1pxu" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1pxu" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Agrin\|Agrin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:48, 10 September 2015

OCA — Thu, 10 Sep 2015 15:48:31 GMT

←Older revision		Revision as of 15:48, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1pxu' size='340' side='right' caption='[[1pxu]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='1pxu' size='340' side='right' caption='[[1pxu]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1pxu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Gallus_gallus Gallus gallus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PXU FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1pxu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PXU FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1jb3\|1jb3]], [[1jc7\|1jc7]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1jb3\|1jb3]], [[1jc7\|1jc7]]</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=1pxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pxu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pxu RCSB], [http://www.ebi.ac.uk/pdbsum/1pxu 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=1pxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pxu OCA], [http://pdbe.org/1pxu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pxu RCSB], [http://www.ebi.ac.uk/pdbsum/1pxu PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 16:
	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 1pxu" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 23:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Gallus gallus~~]]	+	[[Category: Chick]]
	[[Category: Stetefeld, J]]		[[Category: Stetefeld, J]]
	[[Category: Agrin]]		[[Category: Agrin]]
	[[Category: Structural protein]]		[[Category: Structural protein]]

OCA at 02:26, 25 December 2014

OCA — Thu, 25 Dec 2014 02:26:36 GMT

←Older revision		Revision as of 02:26, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1pxu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PXU FirstGlance]. <br>		<table><tr><td colspan='2'>[[1pxu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PXU FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1jb3\|1jb3]], [[1jc7\|1jc7]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1jb3\|1jb3]], [[1jc7\|1jc7]]</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=1pxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pxu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pxu RCSB], [http://www.ebi.ac.uk/pdbsum/1pxu 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=1pxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pxu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pxu RCSB], [http://www.ebi.ac.uk/pdbsum/1pxu PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/AGRIN_CHICK AGRIN_CHICK]] Isoform 1: heparan sulfate basal lamina glycoprotein that plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ) and directs key events in postsynaptic differentiation. Component of the AGRN-LRP4 receptor complex that induces the phosphorylation and activation of MUSK. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Calcium ions are required for maximal AChR clustering. AGRN funtion in neurons is highly regulated by alternative splicing, glycan binding and proteolytic processing. Modulates calcium ion homestasis in neurons, specifically by inducing an increase in cytoplasmic calcium ions. Functions differentially in the central nervous system (CNS) by inhibiting the alpha(3)-subtype of Na+/K+-ATPase and evoking depolarization at CNS synapses.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref> Isoform 9: transmembrane agrin (TM-agrin), the predominant form in neurons of the brain, induces dendritic filopodia and synapse formation in mature hippocampal neurons in large part due to the attached glycosaminoglycan chains and the action of Rho-family GTPases.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref> Isoform 2, isoform 4 and isoform 7: muscle agrin isoforms, which lack the 8-amino acid insert at the 'B' site, but with the insert at the'A' site have no AChr clustering activity nor MUSK activation but bind heparin. Bind alpha-dystroglycan with lower affinity.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref> Isoform 5: muscle agrin A0B0 lacking inserts at both 'A' and 'B' sites has no heparin-binding nor AChR clustering activity but binds strongly alpha-dystroglycan.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref> Agrin N-terminal 110 kDa subunit: is involved in modulation of growth factor signaling (By similarity). Involved also in the regulation of neurite outgrowth probably due to the presence of the glycosaminoglcan (GAG) side chains of heparan and chondroitin sulfate attached to the Ser/Thr- and Gly/Ser-rich regions. Also involved in modulation of growth factor signaling.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref> Agrin C-terminal 22 kDa fragment: this released fragment is important for agrin signaling and to exert a maximal dendritic filopodia-inducing effect. All 'B' splice variants of this fragment also show an increase in the number of filopodia.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 24:
	</StructureSection>		</StructureSection>
	[[Category: Gallus gallus]]		[[Category: Gallus gallus]]
-	[[Category: Stetefeld, J.]]	+	[[Category: Stetefeld, J]]
	[[Category: Agrin]]		[[Category: Agrin]]
	[[Category: Structural protein]]		[[Category: Structural protein]]

OCA at 00:01, 29 September 2014

OCA — Mon, 29 Sep 2014 00:01:16 GMT

←Older revision		Revision as of 00:01, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1pxu.~~png~~\|~~left~~\|~~200px~~]]	+	==Crystal structure of chicken NtA from a eukaryotic source at 2.2A resolution==
		+	<StructureSection load='1pxu' size='340' side='right' caption='[[1pxu]], [[Resolution\|resolution]] 2.20Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1pxu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PXU FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1jb3\|1jb3]], [[1jc7\|1jc7]]</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=1pxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pxu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pxu RCSB], [http://www.ebi.ac.uk/pdbsum/1pxu PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Agrin is a key organizer for postsynaptic differentiation at the neuromuscular junction (NMJ). This activity requires the binding of agrin to the synaptic basal lamina via its N-terminal (NtA) domain. It has been suggested that this binding is mediated by conserved amino acids in the gamma 1 chain of laminin. Here, we report the crystal structure of chicken NtA expressed in eukaryotic HEK293 cells. In contrast to the previously published structure [Stetefeld, J., Jenny, M., Schulthess, T., Landwehr, R., Schumacher, B., Frank, S., Ruegg, M.A., Engel, J., Kammerer, R.A., 2001. The laminin-binding domain of agrin is structurally related to N-TIMP-1. Nat. Struct. Biol., 8, 705-709.], which was derived from the NtA domain expressed in E. coli, the new data show that the N-terminal tail region (amino acid residues Asn1-Arg5) is highly structured. Moreover, the disulfide bridge between Cys2 and Cys74 was also present. In addition, we show that the binding of NtA requires the gamma 1 chain of laminin and is not greatly affected by the composition of beta chains. These results confirm a model of the NtA-laminin complex where conserved amino acids in the gamma 1 chain are prerequisite for the binding to agrin and they further emphasize that the source of protein can be critical in structure determination.

-	~~{{STRUCTURE_1pxu\| PDB=1pxu \| SCENE= }}~~	+	Structure and laminin-binding specificity of the NtA domain expressed in eukaryotic cells.,Mascarenhas JB, Ruegg MA, Sasaki T, Eble JA, Engel J, Stetefeld J Matrix Biol. 2005 Jan;23(8):507-13. Epub 2004 Dec 30. PMID:15694127<ref>PMID:15694127</ref>

-	~~===Crystal structure~~ of ~~chicken NtA from a eukaryotic source at 2~~.~~2A resolution===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_15694127}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1pxu]] is a 1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org~~/~~wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXU OCA].~~	+

	==See Also==		==See Also==
	*[[Agrin\|Agrin]]		*[[Agrin\|Agrin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:015694127<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Gallus gallus]]		[[Category: Gallus gallus]]
	[[Category: Stetefeld, J.]]		[[Category: Stetefeld, J.]]
	[[Category: Agrin]]		[[Category: Agrin]]
	[[Category: Structural protein]]		[[Category: Structural protein]]

OCA at 11:37, 20 October 2012

OCA — Sat, 20 Oct 2012 11:37:49 GMT

←Older revision		Revision as of 11:37, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1pxu]] is a 1 chain structure ~~of [[Agrin]]~~ with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXU OCA].	+	[[1pxu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXU OCA].

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

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

OCA — Thu, 26 Jul 2012 06:01:58 GMT

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

←Older revision

Revision as of 06:01, 26 July 2012