2v5t: Difference between revisions

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<StructureSection load='2v5t' size='340' side='right'caption='[[2v5t]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='2v5t' size='340' side='right'caption='[[2v5t]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2v5t]] 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=2V5T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V5T FirstGlance]. <br>
<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='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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2xy2|2xy2]], [[2jll|2jll]], [[2vaj|2vaj]], [[2doc|2doc]], [[2xyc|2xyc]], [[2wim|2wim]], [[2xy1|2xy1]]</div></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>
<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>
</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.  
[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]]
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   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v5/2v5t_consurf.spt"</scriptWhenChecked>
     <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/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Berezin, V]]
[[Category: Berezin V]]
[[Category: Bock, E]]
[[Category: Bock E]]
[[Category: Gajhede, M]]
[[Category: Gajhede M]]
[[Category: Kristensen, O]]
[[Category: Kristensen O]]
[[Category: Kulahin, N]]
[[Category: Kulahin N]]
[[Category: Rasmussen, K K]]
[[Category: Rasmussen KK]]
[[Category: Walmod, P S]]
[[Category: Walmod PS]]
[[Category: Cell adhesion]]
[[Category: Glycoprotein]]
[[Category: Immunoglobulin domain]]
[[Category: Membrane]]
[[Category: Neural cell adhesion molecule]]
[[Category: Phosphorylation]]
[[Category: Transmembrane]]

Latest revision as of 04:26, 21 November 2024

Crystal structure of NCAM2 Ig2-3Crystal structure of NCAM2 Ig2-3

Structural highlights

2v5t is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Kulahin N, Kristensen O, Rasmussen KK, Olsen L, Rydberg P, Vestergaard B, Kastrup JS, Berezin V, Bock E, Walmod PS, Gajhede M. Structural Model and trans-Interaction of the Entire Ectodomain of the Olfactory Cell Adhesion Molecule. Structure. 2011 Feb 9;19(2):203-11. PMID:21300289 doi:10.1016/j.str.2010.12.014

2v5t, resolution 2.00Å

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