5mc9: Difference between revisions

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

OCA

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-'''Unreleased structure'''
-The entry 5mc9 is ON HOLD  until Paper Publication
+==Crystal structure of the heterotrimeric integrin-binding region of laminin-111==
+<StructureSection load='5mc9' size='340' side='right'caption='[[5mc9]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5mc9]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MC9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MC9 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]] 2.13&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=5mc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mc9 OCA], [https://pdbe.org/5mc9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mc9 RCSB], [https://www.ebi.ac.uk/pdbsum/5mc9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mc9 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/LAMA1_MOUSE LAMA1_MOUSE] 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;">
+== Publication Abstract from PubMed ==
+Laminins are cell-adhesive glycoproteins that are essential for basement membrane assembly and function. Integrins are important laminin receptors, but their binding site on the heterotrimeric laminins is poorly defined structurally. We report the crystal structure at 2.13 A resolution of a minimal integrin-binding fragment of mouse laminin-111, consisting of approximately 50 residues of alpha1beta1gamma1 coiled coil and the first three laminin G-like (LG) domains of the alpha1 chain. The LG domains adopt a triangular arrangement, with the C terminus of the coiled coil situated between LG1 and LG2. The critical integrin-binding glutamic acid residue in the gamma1 chain tail is surface exposed and predicted to bind to the metal ion-dependent adhesion site in the integrin beta1 subunit. Additional contacts to the integrin are likely to be made by the LG1 and LG2 surfaces adjacent to the gamma1 chain tail, which are notably conserved and free of obstructing glycans.
-Authors:
+Crystal Structure of the Heterotrimeric Integrin-Binding Region of Laminin-111.,Pulido D, Hussain SA, Hohenester E Structure. 2017 Mar 7;25(3):530-535. doi: 10.1016/j.str.2017.01.002. Epub 2017, Jan 26. PMID:28132784<ref>PMID:28132784</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5mc9" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Laminin|Laminin]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Mus musculus]]
+[[Category: Hohenester E]]
+[[Category: Pulido D]]