3i70

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{{Seed}}
 
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[[Image:3i70.jpg|left|200px]]
 
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==Long-wavelength structure of NtA==
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The line below this paragraph, containing "STRUCTURE_3i70", creates the "Structure Box" on the page.
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<StructureSection load='3i70' size='340' side='right'caption='[[3i70]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3i70]] 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=3I70 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3I70 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3i70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i70 OCA], [https://pdbe.org/3i70 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3i70 RCSB], [https://www.ebi.ac.uk/pdbsum/3i70 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3i70 ProSAT]</span></td></tr>
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{{STRUCTURE_3i70| PDB=3i70 | SCENE= }}
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i7/3i70_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3i70 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Agrin is a multidomain heparan sulfate proteoglycan involved in postsynaptic differentiation at the neuromuscular junction. Binding of agrin to synaptic basal lamina is mediated by the N-terminal agrin (NtA) domain. The NtA domain of agrin is followed by a tandem of nine follistatin-like (FS) domains forming a rod-like spacer to the laminin G-like domains of the molecule. Here we report that the most C-terminal cysteine residue of NtA (Cys123) forms an interdomain disulfide bond with the FOLN subdomain of the FS module. Remarkably, this single cysteine is flanked by Leu117 and Val124, which are two essential beta-branched amino acids forming the heterocomplex of NtA with the gamma 1 chain of laminin. Moreover, we show that this covalent linkage compensates for the seven amino acid residue splice insert at the very C-terminal helix H3 and causes a rigid interface between NtA and FS independent of the alternative mRNA splice event. These results suggest that the interdomain disulfide bond between the NtA and the first FS domain might be important for the proper folding of agrin.
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===Long-wavelength structure of NtA===
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An interdomain disulfide bridge links the NtA and first FS domain in agrin.,McFarlane AA, Stetefeld J Protein Sci. 2009 Dec;18(12):2421-8. PMID:19845005<ref>PMID:19845005</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3i70" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19845005}}, adds the Publication Abstract to the page
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*[[Agrin|Agrin]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19845005 is the PubMed ID number.
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*[[Agrin 3D structures|Agrin 3D structures]]
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== References ==
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{{ABSTRACT_PUBMED_19845005}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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3I70 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=3I70 OCA].
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==Reference==
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<ref group="xtra">PMID:19845005</ref><references group="xtra"/>
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
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[[Category: Stetefeld, J.]]
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[[Category: Large Structures]]
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[[Category: Alternative splicing]]
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[[Category: Stetefeld J]]
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[[Category: Disulfide bond]]
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[[Category: Egf-like domain]]
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[[Category: Extracelluar matrix]]
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[[Category: Extracellular matrix]]
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[[Category: Glycoprotein]]
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[[Category: Heparan sulfate]]
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[[Category: Laminin binding protein]]
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[[Category: Laminin egf-like domain]]
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[[Category: Proteoglycan]]
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[[Category: Secreted]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 3 16:46:40 2010''
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Current revision

Long-wavelength structure of NtA

PDB ID 3i70

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