View source for 3ncm


==NEURAL CELL ADHESION MOLECULE, MODULE 2, NMR, 20 STRUCTURES==
<StructureSection load='3ncm' size='340' side='right'caption='[[3ncm]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ncm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NCM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NCM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=3ncm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ncm OCA], [https://pdbe.org/3ncm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ncm RCSB], [https://www.ebi.ac.uk/pdbsum/3ncm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ncm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NCAM1_MOUSE NCAM1_MOUSE] This protein is a cell adhesion molecule involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nc/3ncm_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=3ncm ConSurf].
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== Publication Abstract from PubMed ==
The structure in solution of the second Ig-module fragment of residues 117-208 of NCAM has been determined. Like the first Ig-module of residues 20-116, it belongs to the I set of the immunogloblin superfamily. Module 1 and module 2 interact weakly, and the binding sites of this interaction have been identified. The two-module fragment NCAM(20-208) is a stable dimer. Removal of the charged residues in these sites in NCAM(20-208) abolishes the dimerization. Modeling the dimer of NCAM(20-208) to fit the interactions of these charges produces one coherent binding site for the formation of two antiparallel strands of the first two NCAM modules. This mode of binding could be a major element in trans-cellular interactions in neural cell adhesion.

Structure and interactions of NCAM modules 1 and 2, basic elements in neural cell adhesion.,Jensen PH, Soroka V, Thomsen NK, Ralets I, Berezin V, Bock E, Poulsen FM Nat Struct Biol. 1999 May;6(5):486-93. PMID:10331878<ref>PMID:10331878</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Berezin V]]
[[Category: Bock E]]
[[Category: Jensen PH]]
[[Category: Poulsen FM]]
[[Category: Soroka V]]
[[Category: Thomsen NK]]