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| | <StructureSection load='2zou' size='340' side='right'caption='[[2zou]], [[Resolution|resolution]] 1.45Å' scene=''> | | <StructureSection load='2zou' size='340' side='right'caption='[[2zou]], [[Resolution|resolution]] 1.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2zou]] is a 2 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=2ZOU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZOU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2zou]] is a 2 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=2ZOU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZOU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 1.45Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2zot|2zot]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SPON1, KIAA0762, VSGP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2zou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zou OCA], [https://pdbe.org/2zou PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zou RCSB], [https://www.ebi.ac.uk/pdbsum/2zou PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zou 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=2zou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zou OCA], [https://pdbe.org/2zou PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zou RCSB], [https://www.ebi.ac.uk/pdbsum/2zou PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zou ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/SPON1_HUMAN SPON1_HUMAN]] Cell adhesion protein that promotes the attachment of spinal cord and sensory neuron cells and the outgrowth of neurites in vitro. May contribute to the growth and guidance of axons in both the spinal cord and the PNS (By similarity). Major factor for vascular smooth muscle cell.
| + | [https://www.uniprot.org/uniprot/SPON1_HUMAN SPON1_HUMAN] Cell adhesion protein that promotes the attachment of spinal cord and sensory neuron cells and the outgrowth of neurites in vitro. May contribute to the growth and guidance of axons in both the spinal cord and the PNS (By similarity). Major factor for vascular smooth muscle cell. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Nagae, M]] | + | [[Category: Nagae M]] |
| - | [[Category: Nogi, T]] | + | [[Category: Nogi T]] |
| - | [[Category: Takagi, J]] | + | [[Category: Takagi J]] |
| - | [[Category: Beta-sandwich]]
| + | |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Extracellular matrix]]
| + | |
| - | [[Category: Extracellular protein]]
| + | |
| - | [[Category: Glycoprotein]]
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| - | [[Category: Secreted]]
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| Structural highlights
Function
SPON1_HUMAN Cell adhesion protein that promotes the attachment of spinal cord and sensory neuron cells and the outgrowth of neurites in vitro. May contribute to the growth and guidance of axons in both the spinal cord and the PNS (By similarity). Major factor for vascular smooth muscle cell.
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
F-spondin is a secreted and extracellular matrix-attached protein that has been implicated in axonal pathfinding during neural development as well as in vascular remodelling in adult tissues. F-spondin is composed of a reeler, a spondin and six thrombospondin type 1 repeat domains. The reeler domain shares homology with the amino-terminal domain of reelin, a large secreted glycoprotein that guides migrating neurons during cortical development. Crystal structures of the F-spondin reeler domain were determined at 1.45 and 2.70 A resolution. The structure revealed a nine-stranded antiparallel beta-sandwich fold similar to the immunoglobulin or fibronectin type III domains, but with a unique extra beta-hairpin. Moreover, an amino-terminal extension which is anchored at its beginning via a conserved disulfide bond loosely packs against one face of the beta-sandwich, making a major contribution to the surface features of the domain. Structural comparison among the different molecules contained in two different crystals reveals an unusual conformational plasticity of the amino-terminal loop, suggesting its role in molecular interactions.
Structure of the F-spondin reeler domain reveals a unique beta-sandwich fold with a deformable disulfide-bonded loop.,Nagae M, Nishikawa K, Yasui N, Yamasaki M, Nogi T, Takagi J Acta Crystallogr D Biol Crystallogr. 2008 Nov;64(Pt 11):1138-45. Epub 2008, Oct 18. PMID:19020352[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nagae M, Nishikawa K, Yasui N, Yamasaki M, Nogi T, Takagi J. Structure of the F-spondin reeler domain reveals a unique beta-sandwich fold with a deformable disulfide-bonded loop. Acta Crystallogr D Biol Crystallogr. 2008 Nov;64(Pt 11):1138-45. Epub 2008, Oct 18. PMID:19020352 doi:10.1107/S0907444908028308
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