2v5t: Difference between revisions
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==Crystal structure of NCAM2 Ig2-3== | |||
<StructureSection load='2v5t' size='340' side='right'caption='[[2v5t]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2v5t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V5T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V5T FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2v5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v5t OCA], [https://pdbe.org/2v5t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v5t RCSB], [https://www.ebi.ac.uk/pdbsum/2v5t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v5t ProSAT]</span></td></tr> | |||
</table> | |||
== 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 == | |||
[[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/v5/2v5t_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=2v5t ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The 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<ref>PMID:21300289</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2v5t" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Berezin | [[Category: Large Structures]] | ||
[[Category: Bock | [[Category: Berezin V]] | ||
[[Category: Gajhede | [[Category: Bock E]] | ||
[[Category: Kristensen | [[Category: Gajhede M]] | ||
[[Category: Kulahin | [[Category: Kristensen O]] | ||
[[Category: Rasmussen | [[Category: Kulahin N]] | ||
[[Category: Walmod | [[Category: Rasmussen KK]] | ||
[[Category: Walmod PS]] | |||
Latest revision as of 04:26, 21 November 2024
Crystal structure of NCAM2 Ig2-3Crystal structure of NCAM2 Ig2-3
Structural highlights
FunctionNCAM2_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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