5lf2: Difference between revisions
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<StructureSection load='5lf2' size='340' side='right'caption='[[5lf2]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='5lf2' size='340' side='right'caption='[[5lf2]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5lf2]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5lf2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LF2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LF2 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]] 1.85Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5lf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lf2 OCA], [https://pdbe.org/5lf2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lf2 RCSB], [https://www.ebi.ac.uk/pdbsum/5lf2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lf2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/LAMB2_RAT LAMB2_RAT] Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Rattus norvegicus]] | ||
[[Category: | [[Category: Hohenester E]] | ||
[[Category: | [[Category: Pulido D]] | ||
Latest revision as of 11:58, 11 October 2023
Crystal structure of laminin beta2 LE5-LF-LE6Crystal structure of laminin beta2 LE5-LF-LE6
Structural highlights
FunctionLAMB2_RAT Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Publication Abstract from PubMedLaminins are a major constituent of all basement membranes. The polymerisation of laminins at the cell surface is mediated by the three short arms of the cross-shaped laminin heterotrimer. The short arms contain repeats of laminin-type epidermal growth factor-like (LE) domains, interspersed with globular domains of unknown function. A single LF domain is inserted between LE5 and LE6 of the laminin beta1 and beta2 chains. We report the crystal structure at 1.85A resolution of the laminin beta2 LE5-LF-LE6 region. The LF domain consists of a beta-sandwich related to bacterial family 35 carbohydrate binding modules, and more distantly to the L4 domains present in the short arms of laminin alpha and gamma chains. An alpha-helical region mediates the extensive interaction of the LF domain with LE5. The relative arrangement of LE5 and LE6 is very similar to that of consecutive LE domains in uninterrupted LE tandems. Fitting atomic models to a low-resolution structure of the first eight domains of the laminin beta1 chain determined by small-angle X-ray scattering suggests a deviation from the regular LE array at the LE4-LE5 junction. These results advance our understanding of laminin structure. Crystallographic analysis of the laminin beta2 short arm reveals how the LF domain is inserted into a regular array of LE domains.,Pulido D, Briggs DC, Hua J, Hohenester E Matrix Biol. 2016 Jul 16. pii: S0945-053X(16)30079-8. doi:, 10.1016/j.matbio.2016.06.006. PMID:27425256[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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