2jll: Difference between revisions
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<StructureSection load='2jll' size='340' side='right'caption='[[2jll]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='2jll' size='340' side='right'caption='[[2jll]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2jll]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2jll]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JLL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JLL 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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | </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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2v5t|2v5t]], [[2xy2|2xy2]], [[2vaj|2vaj]], [[2doc|2doc]], [[2xyc|2xyc]], [[2wim|2wim]], [[2xy1|2xy1]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2v5t|2v5t]], [[2xy2|2xy2]], [[2vaj|2vaj]], [[2doc|2doc]], [[2xyc|2xyc]], [[2wim|2wim]], [[2xy1|2xy1]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jll OCA], [https://pdbe.org/2jll PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jll RCSB], [https://www.ebi.ac.uk/pdbsum/2jll PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jll ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/NCAM2_HUMAN NCAM2_HUMAN]] May play important roles in selective fasciculation and zone-to-zone projection of the primary olfactory axons. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Latest revision as of 11:14, 19 January 2022
Crystal structure of NCAM2 IgIV-FN3IICrystal structure of NCAM2 IgIV-FN3II
Structural highlights
Function[NCAM2_HUMAN] May play important roles in selective fasciculation and zone-to-zone projection of the primary olfactory axons. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe ectodomain of olfactory cell adhesion molecule (OCAM/NCAM2/RNCAM) consists of five immunoglobulin (Ig) domains (IgI-V), followed by two fibronectin-type 3 (Fn3) domains (Fn3I-II). A complete structural model of the entire ectodomain of human OCAM has been assembled from crystal structures of six recombinant proteins corresponding to different regions of the ectodomain. The model is the longest experimentally based composite structural model of an entire IgCAM ectodomain. It displays an essentially linear arrangement of IgI-V, followed by bends between IgV and Fn3I and between Fn3I and Fn3II. Proteins containing IgI-IgII domains formed stable homodimers in solution and in crystals. Dimerization could be disrupted in vitro by mutations in the dimer interface region. In conjunction with the bent ectodomain conformation, which can position IgI-V parallel with the cell surface, the IgI-IgII dimerization enables OCAM-mediated trans-interactions with an intercellular distance of about 20 nm, which is consistent with that observed in synapses. Structural Model and trans-Interaction of the Entire Ectodomain of the Olfactory Cell Adhesion Molecule.,Kulahin N, Kristensen O, Rasmussen KK, Olsen L, Rydberg P, Vestergaard B, Kastrup JS, Berezin V, Bock E, Walmod PS, Gajhede M Structure. 2011 Feb 9;19(2):203-11. PMID:21300289[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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