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==CRYSTAL STRUCTURE OF TANDEM TYPE III FIBRONECTIN DOMAINS FROM DROSOPHILA NEUROGLIAN AT 2.0 ANGSTROMS== | |||
<StructureSection load='1cfb' size='340' side='right'caption='[[1cfb]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
| | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1cfb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CFB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CFB 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=NA:SODIUM+ION'>NA</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=1cfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cfb OCA], [https://pdbe.org/1cfb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cfb RCSB], [https://www.ebi.ac.uk/pdbsum/1cfb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cfb ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/NRG_DROME NRG_DROME] The long isoform may play a role in neural and glial cell adhesion in the developing embryo. The short isoform may be a more general cell adhesion molecule involved in other tissues and imaginal disk morphogenesis. Vital for embryonic development. Essential for septate junctions. Septate junctions, which are the equivalent of vertebrates tight junctions, are characterized by regular arrays of transverse structures that span the intermembrane space and form a physical barrier to diffusion. Required for the blood-brain barrier formation.<ref>PMID:1693086</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/cf/1cfb_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=1cfb ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We report the crystal structure of two adjacent fibronectin type III repeats from the Drosophila neural cell adhesion molecule neuroglian. Each domain consists of two antiparallel beta sheets and is folded topologically identically to single fibronectin type III domains from the extracellular matrix proteins tenascin and fibronectin. beta bulges and left-handed polyproline II helices disrupt the regular beta sheet structure of both neuroglian domains. The hydrophobic interdomain interface includes a metal-binding site, presumably involved in stabilizing the relative orientation between domains and predicted by sequence comparision to be present in the vertebrate homolog molecule L1. The neuroglian domains are related by a near perfect 2-fold screw axis along the longest molecular dimension. Using this relationship, a model for arrays of tandem fibronectin type III repeats in neuroglian and other molecules is proposed. | We report the crystal structure of two adjacent fibronectin type III repeats from the Drosophila neural cell adhesion molecule neuroglian. Each domain consists of two antiparallel beta sheets and is folded topologically identically to single fibronectin type III domains from the extracellular matrix proteins tenascin and fibronectin. beta bulges and left-handed polyproline II helices disrupt the regular beta sheet structure of both neuroglian domains. The hydrophobic interdomain interface includes a metal-binding site, presumably involved in stabilizing the relative orientation between domains and predicted by sequence comparision to be present in the vertebrate homolog molecule L1. The neuroglian domains are related by a near perfect 2-fold screw axis along the longest molecular dimension. Using this relationship, a model for arrays of tandem fibronectin type III repeats in neuroglian and other molecules is proposed. | ||
Crystal structure of tandem type III fibronectin domains from Drosophila neuroglian at 2.0 A.,Huber AH, Wang YM, Bieber AJ, Bjorkman PJ Neuron. 1994 Apr;12(4):717-31. PMID:7512815<ref>PMID:7512815</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1cfb" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Bieber | [[Category: Bieber AJ]] | ||
[[Category: Bjorkman | [[Category: Bjorkman PJ]] | ||
[[Category: Huber | [[Category: Huber AH]] | ||
[[Category: Wang | [[Category: Wang YE]] | ||
Latest revision as of 09:29, 30 October 2024
CRYSTAL STRUCTURE OF TANDEM TYPE III FIBRONECTIN DOMAINS FROM DROSOPHILA NEUROGLIAN AT 2.0 ANGSTROMSCRYSTAL STRUCTURE OF TANDEM TYPE III FIBRONECTIN DOMAINS FROM DROSOPHILA NEUROGLIAN AT 2.0 ANGSTROMS
Structural highlights
FunctionNRG_DROME The long isoform may play a role in neural and glial cell adhesion in the developing embryo. The short isoform may be a more general cell adhesion molecule involved in other tissues and imaginal disk morphogenesis. Vital for embryonic development. Essential for septate junctions. Septate junctions, which are the equivalent of vertebrates tight junctions, are characterized by regular arrays of transverse structures that span the intermembrane space and form a physical barrier to diffusion. Required for the blood-brain barrier formation.[1] 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 PubMedWe report the crystal structure of two adjacent fibronectin type III repeats from the Drosophila neural cell adhesion molecule neuroglian. Each domain consists of two antiparallel beta sheets and is folded topologically identically to single fibronectin type III domains from the extracellular matrix proteins tenascin and fibronectin. beta bulges and left-handed polyproline II helices disrupt the regular beta sheet structure of both neuroglian domains. The hydrophobic interdomain interface includes a metal-binding site, presumably involved in stabilizing the relative orientation between domains and predicted by sequence comparision to be present in the vertebrate homolog molecule L1. The neuroglian domains are related by a near perfect 2-fold screw axis along the longest molecular dimension. Using this relationship, a model for arrays of tandem fibronectin type III repeats in neuroglian and other molecules is proposed. Crystal structure of tandem type III fibronectin domains from Drosophila neuroglian at 2.0 A.,Huber AH, Wang YM, Bieber AJ, Bjorkman PJ Neuron. 1994 Apr;12(4):717-31. PMID:7512815[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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