1epf: Difference between revisions

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<StructureSection load='1epf' size='340' side='right'caption='[[1epf]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='1epf' size='340' side='right'caption='[[1epf]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1epf]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EPF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EPF FirstGlance]. <br>
<table><tr><td colspan='2'>[[1epf]] is a 4 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=1EPF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EPF 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></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]] 1.85&#8491;</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></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=1epf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1epf OCA], [https://pdbe.org/1epf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1epf RCSB], [https://www.ebi.ac.uk/pdbsum/1epf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1epf 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=1epf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1epf OCA], [https://pdbe.org/1epf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1epf RCSB], [https://www.ebi.ac.uk/pdbsum/1epf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1epf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/NCAM1_RAT NCAM1_RAT]] This protein is a cell adhesion molecule involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc.  
[https://www.uniprot.org/uniprot/NCAM1_RAT NCAM1_RAT] This protein is a cell adhesion molecule involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc.
== 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=1epf 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=1epf ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The neural cell adhesion molecule NCAM, a member of the immunoglobulin superfamily, mediates cell-cell recognition and adhesion via a homophilic interaction. NCAM plays a key role during development and regeneration of the nervous system and is involved in synaptic plasticity associated with memory and learning. The 1.85 A crystal structure of the two N-terminal extracellular domains of NCAM reported here provides a structural basis for the homophilic interaction. The molecular packing of the two-domain structure reveals a cross shaped antiparallel dimer, and provides fundamental insight into trans-cellular recognition mediated by NCAM.
Structural basis of cell-cell adhesion by NCAM.,Kasper C, Rasmussen H, Kastrup JS, Ikemizu S, Jones EY, Berezin V, Bock E, Larsen IK Nat Struct Biol. 2000 May;7(5):389-93. PMID:10802736<ref>PMID:10802736</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1epf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Berezin, V]]
[[Category: Rattus norvegicus]]
[[Category: Bock, E]]
[[Category: Berezin V]]
[[Category: Ikemizu, S]]
[[Category: Bock E]]
[[Category: Jones, E Y]]
[[Category: Ikemizu S]]
[[Category: Kasper, C]]
[[Category: Jones EY]]
[[Category: Kastrup, J S]]
[[Category: Kasper C]]
[[Category: Larsen, I K]]
[[Category: Kastrup JS]]
[[Category: Rasmussen, H]]
[[Category: Larsen IK]]
[[Category: Cell adhesion]]
[[Category: Rasmussen H]]
[[Category: Glycoprotein]]
[[Category: Immunoglobulin fold]]
[[Category: Ncam]]
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