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<StructureSection load='1olz' size='340' side='right'caption='[[1olz]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1olz' size='340' side='right'caption='[[1olz]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1olz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OLZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OLZ FirstGlance]. <br>
<table><tr><td colspan='2'>[[1olz]] 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=1OLZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OLZ FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1olz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1olz OCA], [http://pdbe.org/1olz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1olz RCSB], [http://www.ebi.ac.uk/pdbsum/1olz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1olz ProSAT]</span></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1olz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1olz OCA], [https://pdbe.org/1olz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1olz RCSB], [https://www.ebi.ac.uk/pdbsum/1olz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1olz ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SEM4D_HUMAN SEM4D_HUMAN]] Cell surface receptor for PLXN1B and PLXNB2 that plays an important role in cell-cell signaling. Promotes reorganization of the actin cytoskeleton and plays a role in axonal growth cone guidance in the developing central nervous system. Regulates dendrite and axon branching and morphogenesis. Promotes the migration of cerebellar granule cells and of endothelial cells. Plays a role in the immune system; induces B-cells to aggregate and improves their viability (in vitro). Promotes signaling via SRC and PTK2B/PYK2, which then mediates activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade. Interaction with PLXNB1 mediates activation of RHOA.<ref>PMID:16055703</ref> <ref>PMID:19788569</ref> <ref>PMID:20877282</ref> <ref>PMID:8876214</ref>
[https://www.uniprot.org/uniprot/SEM4D_HUMAN SEM4D_HUMAN] Cell surface receptor for PLXN1B and PLXNB2 that plays an important role in cell-cell signaling. Promotes reorganization of the actin cytoskeleton and plays a role in axonal growth cone guidance in the developing central nervous system. Regulates dendrite and axon branching and morphogenesis. Promotes the migration of cerebellar granule cells and of endothelial cells. Plays a role in the immune system; induces B-cells to aggregate and improves their viability (in vitro). Promotes signaling via SRC and PTK2B/PYK2, which then mediates activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade. Interaction with PLXNB1 mediates activation of RHOA.<ref>PMID:16055703</ref> <ref>PMID:19788569</ref> <ref>PMID:20877282</ref> <ref>PMID:8876214</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1olz ConSurf].
</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=1olz ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Semaphorins, proteins characterized by an extracellular sema domain, regulate axon guidance, immune function and angiogenesis. The crystal structure of SEMA4D (residues 1-657) shows the sema topology to be a seven-bladed beta-propeller, revealing an unexpected homology with integrins. The sema beta-propeller contains a distinctive 77-residue insertion between beta-strands C and D of blade 5. Blade 7 is followed by a domain common to plexins, semaphorins and integrins (PSI domain), which forms a compact cysteine knot abutting the side of the propeller, and an Ig-like domain. The top face of the beta-propeller presents prominent loops characteristic of semaphorins. In addition to limited contact between the Ig-like domains, the homodimer is stabilized through extensive interactions between the top faces in a sector of the beta-propeller used for heterodimerization in integrins. This face of the propeller also mediates ligand binding in integrins, and functional data for semaphorin-receptor interactions map to the equivalent surface.
The ligand-binding face of the semaphorins revealed by the high-resolution crystal structure of SEMA4D.,Love CA, Harlos K, Mavaddat N, Davis SJ, Stuart DI, Jones EY, Esnouf RM Nat Struct Biol. 2003 Oct;10(10):843-8. Epub 2003 Sep 7. PMID:12958590<ref>PMID:12958590</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1olz" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Semaphorin|Semaphorin]]
*[[Semaphorin 3D structures|Semaphorin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Davis, S J]]
[[Category: Davis SJ]]
[[Category: Esnouf, R M]]
[[Category: Esnouf RM]]
[[Category: Harlos, K]]
[[Category: Harlos K]]
[[Category: Jones, E Y]]
[[Category: Jones EY]]
[[Category: Love, C A]]
[[Category: Love CA]]
[[Category: Mavaddat, N]]
[[Category: Mavaddat N]]
[[Category: Stuart, D I]]
[[Category: Stuart DI]]
[[Category: Beta-propeller]]
[[Category: Cd100]]
[[Category: Developmental protein]]
[[Category: Extracellular receptor]]
[[Category: Glycoprotein developmental protein]]
[[Category: Ig-like domain]]
[[Category: Neurogenesis]]
[[Category: Psi domain]]
[[Category: Semaphorin]]
[[Category: Spine]]
[[Category: Structural genomic]]
[[Category: Structural proteomics in europe]]

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