1olz: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1olz.jpg|left|200px]]<br /><applet load="1olz" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1olz, resolution 2.00&Aring;" />
-'''THE LIGAND-BINDING FACE OF THE SEMAPHORINS REVEALED BY THE HIGH RESOLUTION CRYSTAL STRUCTURE OF SEMA4D'''<br />
-==Overview==
+==The ligand-binding face of the semaphorins revealed by the high resolution crystal structure of SEMA4D==
-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.
+<StructureSection load='1olz' size='340' side='right'caption='[[1olz]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<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='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>
+== Function ==
+[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 ==
+[[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/ol/1olz_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1olz ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-OLZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://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].
+*[[Semaphorin 3D structures|Semaphorin 3D structures]]
+== References ==
-==Reference==
+<references/>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12958590 12958590]
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[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: SPINE, Structural Proteomics in Europe.]]
+[[Category: Stuart DI]]
-[[Category: Stuart, D I.]]
-[[Category: beta-propeller]]
-[[Category: cd100]]
-[[Category: extracellular receptor]]
-[[Category: glycoprotein developmental protein]]
-[[Category: ig-like domain]]
-[[Category: neurogenesis]]
-[[Category: psi domain]]
-[[Category: semaphorin]]
-[[Category: spine]]
-[[Category: structural genomics]]
-[[Category: structural proteomics in europe]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:19:07 2008''