1cs6

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<StructureSection load='1cs6' size='340' side='right'caption='[[1cs6]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1cs6' size='340' side='right'caption='[[1cs6]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1cs6]] 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=1CS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CS6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1cs6]] 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=1CS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CS6 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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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]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=1cs6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cs6 OCA], [https://pdbe.org/1cs6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cs6 RCSB], [https://www.ebi.ac.uk/pdbsum/1cs6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cs6 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=1cs6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cs6 OCA], [https://pdbe.org/1cs6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cs6 RCSB], [https://www.ebi.ac.uk/pdbsum/1cs6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cs6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CNTN2_CHICK CNTN2_CHICK]] Axon-associated cell adhesion molecule (AxCAM) which promotes neurite outgrowth by interaction with the AxCAM L1 (G4) of neuritic membrane.
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[https://www.uniprot.org/uniprot/CNTN2_CHICK CNTN2_CHICK] Axon-associated cell adhesion molecule (AxCAM) which promotes neurite outgrowth by interaction with the AxCAM L1 (G4) of neuritic membrane.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1cs6 ConSurf].
</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=1cs6 ConSurf].
<div style="clear:both"></div>
<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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We have determined the crystal structure of the ligand binding fragment of the neural cell adhesion molecule axonin-1/TAG-1 comprising the first four immunoglobulin (Ig) domains. The overall structure of axonin-1(Ig1-4) is U-shaped due to contacts between domains 1 and 4 and domains 2 and 3. In the crystals, these molecules are aligned in a string with adjacent molecules oriented in an anti-parallel fashion and their C termini perpendicular to the string. This arrangement suggests that cell adhesion by homophilic axonin-1 interaction occurs by the formation of a linear zipper-like array in which the axonin-1 molecules are alternately provided by the two apposed membranes. In accordance with this model, mutations in a loop critical for the formation of the zipper resulted in the loss of the homophilic binding capacity of axonin-1.
 
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The crystal structure of the ligand binding module of axonin-1/TAG-1 suggests a zipper mechanism for neural cell adhesion.,Freigang J, Proba K, Leder L, Diederichs K, Sonderegger P, Welte W Cell. 2000 May 12;101(4):425-33. PMID:10830169<ref>PMID:10830169</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 1cs6" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Chick]]
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[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Diederichs, K]]
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[[Category: Diederichs K]]
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[[Category: Freigang, J]]
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[[Category: Freigang J]]
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[[Category: Proba, K]]
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[[Category: Proba K]]
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[[Category: Sonderegger, P]]
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[[Category: Sonderegger P]]
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[[Category: Welte, W]]
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[[Category: Welte W]]
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[[Category: Cell adhesion]]
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[[Category: Neural cell adhesion]]
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Revision as of 15:42, 13 March 2024

N-TERMINAL FRAGMENT OF AXONIN-1 FROM CHICKEN

PDB ID 1cs6

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