5mc9: Difference between revisions

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<StructureSection load='5mc9' size='340' side='right'caption='[[5mc9]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
<StructureSection load='5mc9' size='340' side='right'caption='[[5mc9]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5mc9]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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 [http://proteopedia.org/fgij/fg.htm?mol=5MC9 FirstGlance]. <br>
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Lama1, Lama, Lama-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), Lamb1, Lamb-1, Lamb1-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), Lamc1, Lamb-2, Lamc-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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'>[http://proteopedia.org/fgij/fg.htm?mol=5mc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mc9 OCA], [http://pdbe.org/5mc9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mc9 RCSB], [http://www.ebi.ac.uk/pdbsum/5mc9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mc9 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=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>
</table>
== Function ==
== Function ==
[[http://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. [[http://www.uniprot.org/uniprot/LAMC1_MOUSE LAMC1_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. [[http://www.uniprot.org/uniprot/LAMB1_MOUSE LAMB1_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. Involved in the organization of the laminar architecture of the cerebral cortex (By similarity). It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons (By similarity). Radial glial cells play a central role in cerebral cortical development, where they act both as the proliferative unit of the cerebral cortex and a scaffold for neurons migrating toward the pial surface (By similarity).  
[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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lk3 transgenic mice]]
[[Category: Mus musculus]]
[[Category: Hohenester, E]]
[[Category: Hohenester E]]
[[Category: Pulido, D]]
[[Category: Pulido D]]
[[Category: Cell adhesion]]
[[Category: Coiled coil]]
[[Category: Extracellular matrix]]
[[Category: Laminin g-like domain]]

Latest revision as of 21:38, 1 November 2023

Crystal structure of the heterotrimeric integrin-binding region of laminin-111Crystal structure of the heterotrimeric integrin-binding region of laminin-111

Structural highlights

5mc9 is a 3 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.13Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Pulido D, Hussain SA, Hohenester E. Crystal Structure of the Heterotrimeric Integrin-Binding Region of Laminin-111. Structure. 2017 Mar 7;25(3):530-535. doi: 10.1016/j.str.2017.01.002. Epub 2017, Jan 26. PMID:28132784 doi:http://dx.doi.org/10.1016/j.str.2017.01.002

5mc9, resolution 2.13Å

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