6x38
From Proteopedia
(Difference between revisions)
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<StructureSection load='6x38' size='340' side='right'caption='[[6x38]], [[Resolution|resolution]] 1.30Å' scene=''> | <StructureSection load='6x38' size='340' side='right'caption='[[6x38]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6x38]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[6x38]] 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=6X38 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6X38 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6x38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x38 OCA], [https://pdbe.org/6x38 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6x38 RCSB], [https://www.ebi.ac.uk/pdbsum/6x38 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6x38 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=6x38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x38 OCA], [https://pdbe.org/6x38 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6x38 RCSB], [https://www.ebi.ac.uk/pdbsum/6x38 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6x38 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/LAR_DROME LAR_DROME] Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase). It controls motor axon guidance.<ref>PMID:2554325</ref> <ref>PMID:8598047</ref> | |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
The type IIa family of receptor protein tyrosine phosphatases (RPTPs), including Lar, RPTPsigma and RPTPdelta, are well-studied in coordinating actin cytoskeletal rearrangements during axon guidance and synaptogenesis. To determine whether this regulation is conserved in other tissues, interdisciplinary approaches were utilized to study Lar-RPTPs in the Drosophila musculature. Here we find that the single fly ortholog, Drosophila Lar (Dlar), is localized to the muscle costamere and that a decrease in Dlar causes aberrant sarcomeric patterning, deficits in larval locomotion, and integrin mislocalization. Sequence analysis uncovered an evolutionarily conserved Lys-Gly-Asp (KGD) signature in the extracellular region of Dlar. Since this tripeptide sequence is similar to the integrin-binding Arg-Gly-Asp (RGD) motif, we tested the hypothesis that Dlar directly interacts with integrin proteins. However, structural analyses of the fibronectin type III domains of Dlar and two vertebrate orthologs that include this conserved motif indicate that this KGD tripeptide is not accessible and thus unlikely to mediate physical interactions with integrins. These results, together with the proteomics identification of basement membrane (BM) proteins as potential ligands for type IIa RPTPs, suggest a complex network of protein interactions in the extracellular space that may mediate Lar function and/or signaling in muscle tissue. | The type IIa family of receptor protein tyrosine phosphatases (RPTPs), including Lar, RPTPsigma and RPTPdelta, are well-studied in coordinating actin cytoskeletal rearrangements during axon guidance and synaptogenesis. To determine whether this regulation is conserved in other tissues, interdisciplinary approaches were utilized to study Lar-RPTPs in the Drosophila musculature. Here we find that the single fly ortholog, Drosophila Lar (Dlar), is localized to the muscle costamere and that a decrease in Dlar causes aberrant sarcomeric patterning, deficits in larval locomotion, and integrin mislocalization. Sequence analysis uncovered an evolutionarily conserved Lys-Gly-Asp (KGD) signature in the extracellular region of Dlar. Since this tripeptide sequence is similar to the integrin-binding Arg-Gly-Asp (RGD) motif, we tested the hypothesis that Dlar directly interacts with integrin proteins. However, structural analyses of the fibronectin type III domains of Dlar and two vertebrate orthologs that include this conserved motif indicate that this KGD tripeptide is not accessible and thus unlikely to mediate physical interactions with integrins. These results, together with the proteomics identification of basement membrane (BM) proteins as potential ligands for type IIa RPTPs, suggest a complex network of protein interactions in the extracellular space that may mediate Lar function and/or signaling in muscle tissue. | ||
| - | Complex protein interactions mediate Drosophila Lar function in muscle tissue.,Kawakami J, Brooks D, Zalmai R, Hartson SD, Bouyain S, Geisbrecht ER PLoS One. 2022 May 27;17(5):e0269037. doi: 10.1371/journal.pone.0269037., eCollection 2022. PMID:35622884<ref>PMID:35622884</ref> | + | Complex protein interactions mediate Drosophila Lar function in muscle tissue.,Kawakami J, Brooks D, Zalmai R, Hartson SD, Bouyain S, Geisbrecht ER PLoS One. 2022 May 27;17(5):e0269037. doi: 10.1371/journal.pone.0269037. , eCollection 2022. PMID:35622884<ref>PMID:35622884</ref> |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Drosophila melanogaster]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | + | [[Category: Bouyain S]] | |
| - | [[Category: Bouyain | + | [[Category: Kawakami JE]] |
| - | [[Category: Kawakami | + | |
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Current revision
Crystal structure of the FN5 domain of Drosophila Lar
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