1qu0: Difference between revisions

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[[Image:1qu0.jpg|left|200px]]


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==CRYSTAL STRUCTURE OF THE FIFTH LAMININ G-LIKE MODULE OF THE MOUSE LAMININ ALPHA2 CHAIN==
The line below this paragraph, containing "STRUCTURE_1qu0", creates the "Structure Box" on the page.
<StructureSection load='1qu0' size='340' side='right'caption='[[1qu0]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1qu0]] is a 4 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=1QU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QU0 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
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<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=SO4:SULFATE+ION'>SO4</scene></td></tr>
{{STRUCTURE_1qu0| PDB=1qu0 |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qu0 OCA], [https://pdbe.org/1qu0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qu0 RCSB], [https://www.ebi.ac.uk/pdbsum/1qu0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qu0 ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/LAMA2_MOUSE LAMA2_MOUSE] Note=Defects in Lama2 are a cause of murine muscular dystrophy (dy2J).
== Function ==
[https://www.uniprot.org/uniprot/LAMA2_MOUSE LAMA2_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.
== 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/qu/1qu0_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1qu0 ConSurf].
<div style="clear:both"></div>


'''CRYSTAL STRUCTURE OF THE FIFTH LAMININ G-LIKE MODULE OF THE MOUSE LAMININ ALPHA2 CHAIN'''
==See Also==
 
*[[Laminin|Laminin]]
 
__TOC__
==Overview==
</StructureSection>
Laminin G-like (LG) modules in the extracellular matrix glycoproteins laminin, perlecan, and agrin mediate the binding to heparin and the cell surface receptor alpha-dystroglycan (alpha-DG). These interactions are crucial to basement membrane assembly, as well as muscle and nerve cell function. The crystal structure of the laminin alpha 2 chain LG5 module reveals a 14-stranded beta sandwich. A calcium ion is bound to one edge of the sandwich by conserved acidic residues and is surrounded by residues implicated in heparin and alpha-DG binding. A calcium-coordinated sulfate ion is suggested to mimic the binding of anionic oligosaccharides. The structure demonstrates a conserved function of the LG module in calcium-dependent lectin-like alpha-DG binding.
[[Category: Large Structures]]
 
==About this Structure==
1QU0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QU0 OCA].
 
==Reference==
The crystal structure of a laminin G-like module reveals the molecular basis of alpha-dystroglycan binding to laminins, perlecan, and agrin., Hohenester E, Tisi D, Talts JF, Timpl R, Mol Cell. 1999 Nov;4(5):783-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10619025 10619025]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Hohenester E]]
[[Category: Hohenester, E.]]
[[Category: Talts JF]]
[[Category: Talts, J F.]]
[[Category: Timpl R]]
[[Category: Timpl, R.]]
[[Category: Tisi D]]
[[Category: Tisi, D.]]
[[Category: Beta sandwich]]
[[Category: Calcium-binding protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:42:16 2008''

Latest revision as of 09:07, 17 April 2024

CRYSTAL STRUCTURE OF THE FIFTH LAMININ G-LIKE MODULE OF THE MOUSE LAMININ ALPHA2 CHAINCRYSTAL STRUCTURE OF THE FIFTH LAMININ G-LIKE MODULE OF THE MOUSE LAMININ ALPHA2 CHAIN

Structural highlights

1qu0 is a 4 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 2.35Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

LAMA2_MOUSE Note=Defects in Lama2 are a cause of murine muscular dystrophy (dy2J).

Function

LAMA2_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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1qu0, resolution 2.35Å

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