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1ie5

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(New page: 200px<br /><applet load="1ie5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ie5" /> '''NMR STRUCTURE OF THE THIRD IMMUNOGLOBULIN DO...)
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[[Image:1ie5.gif|left|200px]]<br /><applet load="1ie5" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ie5" />
 
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'''NMR STRUCTURE OF THE THIRD IMMUNOGLOBULIN DOMAIN FROM THE NEURAL CELL ADHESION MOLECULE.'''<br />
 
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==Overview==
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==NMR STRUCTURE OF THE THIRD IMMUNOGLOBULIN DOMAIN FROM THE NEURAL CELL ADHESION MOLECULE.==
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Homophilic binding of the neural cell adhesion molecule (N-CAM) mediates, the calcium-independent cell-cell adhesion that is involved in neuronal, development. Two hypotheses have been advanced for the mechanism of, homophilic binding. Cell-based experiments have implicated each of the, five extracellular immunoglobulin (Ig) domains of N-CAM in the homophilic, adhesion interaction, and have predicted that the third domain (Ig III), self-associates. The alternative hypothesis is based on solution, observations, which implicate a specific antiparallel interaction between, the first two Ig domains (Ig I and Ig II). In order to test these, hypotheses, we have determined a high-resolution solution structure of, recombinant Ig III (sequence derived from chicken N-CAM) and examined the, aggregation behavior of isolated Ig domains in solution. The structure, shows that Ig III adopts a canonical Ig fold, in which the beta strands, ABED and A'GFCC' form two beta sheets that are linked by a disulfide bond., In contrast to the demonstrated aggregation of Ig III on solid supports, we were unable to demonstrate self-association of Ig III under any of a, variety of solution conditions. The structure shows that the surface of Ig, III is dominated by two large acidic patches, which may explain our, failure to observe self-association in solution. To evaluate the, involvement of the Ig I-Ig II interaction in cell-cell adhesion, we, designed a point mutation in Ig I (F19S) that proved sufficient to, abrogate the Ig I-Ig II interaction seen in solution. However, the, introduction of this mutation into full-length N-CAM expressed in COS-7, cells failed to affect N-CAM-mediated cell-cell adhesion. The inability to, observe Ig III self-association in solution, combined with the failure of, the F19S mutation to affect N-CAM-mediated cell-cell adhesion, suggests, that, although solution studies can give important insights into the, structures of individual domains, the interactions observed in solution, between the domains may not be representative of the interactions that, occur on the cell surface.
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<StructureSection load='1ie5' size='340' side='right'caption='[[1ie5]]' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1ie5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IE5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IE5 FirstGlance]. <br>
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1IE5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IE5 OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1ie5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ie5 OCA], [https://pdbe.org/1ie5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ie5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ie5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ie5 ProSAT]</span></td></tr>
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==Reference==
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</table>
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Solution structure of the third immunoglobulin domain of the neural cell adhesion molecule N-CAM: can solution studies define the mechanism of homophilic binding?, Atkins AR, Chung J, Deechongkit S, Little EB, Edelman GM, Wright PE, Cunningham BA, Dyson HJ, J Mol Biol. 2001 Aug 3;311(1):161-72. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11469865 11469865]
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== Function ==
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[https://www.uniprot.org/uniprot/NCAM1_CHICK NCAM1_CHICK] This protein is a cell adhesion molecule involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc.
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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/ie/1ie5_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=1ie5 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Atkins, A.R.]]
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[[Category: Atkins AR]]
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[[Category: Chung, J.]]
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[[Category: Chung J]]
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[[Category: Cunningham, B.A.]]
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[[Category: Cunningham BA]]
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[[Category: Deechongkit, S.]]
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[[Category: Deechongkit S]]
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[[Category: Dyson, H.J.]]
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[[Category: Dyson HJ]]
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[[Category: Edelman, G.M.]]
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[[Category: Edelman GM]]
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[[Category: Little, E.B.]]
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[[Category: Little EB]]
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[[Category: Wright, P.E.]]
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[[Category: Wright PE]]
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[[Category: intermediate immunoglobulin fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:20:03 2007''
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Current revision

NMR STRUCTURE OF THE THIRD IMMUNOGLOBULIN DOMAIN FROM THE NEURAL CELL ADHESION MOLECULE.

PDB ID 1ie5

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