This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

5xau

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Crystal structure of integrin binding fragment of laminin-511

Structural highlights

5xau is a 6 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	LAMA5, KIAA0533, KIAA1907 (HUMAN), LAMB1 (HUMAN), LAMC1, LAMB2 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[LAMB1_HUMAN] Cobblestone lissencephaly without muscular or ocular involvement. The disease is caused by mutations affecting the gene represented in this entry.

Function

[LAMA5_HUMAN] 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. [LAMC1_HUMAN] 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. [LAMB1_HUMAN] 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 cerebral cortex. 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. 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.^[1]

Publication Abstract from PubMed

Laminins regulate diverse cellular functions through interaction with integrins. Two regions of laminins-three laminin globular domains of the alpha chain (LG1-3) and the carboxyl-terminal tail of the gamma chain (gamma-tail)-are required for integrin binding, but it remains unclear how the gamma-tail contributes to the binding. We determined the crystal structure of the integrin binding fragment of laminin-511, showing that the gamma-tail extends to the bottom face of LG1-3. Electron microscopic imaging combined with biochemical analyses showed that integrin binds to the bottom face of LG1-3 with the gamma1-tail apposed to the metal ion-dependent adhesion site (MIDAS) of integrin beta1. These findings are consistent with a model in which the gamma-tail coordinates the metal ion in the MIDAS through its Glu residue.

Mechanistic basis for the recognition of laminin-511 by alpha6beta1 integrin.,Takizawa M, Arimori T, Taniguchi Y, Kitago Y, Yamashita E, Takagi J, Sekiguchi K Sci Adv. 2017 Sep 1;3(9):e1701497. doi: 10.1126/sciadv.1701497. eCollection 2017 , Sep. PMID:28879238^[2]

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

References

↑ Radmanesh F, Caglayan AO, Silhavy JL, Yilmaz C, Cantagrel V, Omar T, Rosti B, Kaymakcalan H, Gabriel S, Li M, Sestan N, Bilguvar K, Dobyns WB, Zaki MS, Gunel M, Gleeson JG. Mutations in LAMB1 cause cobblestone brain malformation without muscular or ocular abnormalities. Am J Hum Genet. 2013 Mar 7;92(3):468-74. doi: 10.1016/j.ajhg.2013.02.005. PMID:23472759 doi:http://dx.doi.org/10.1016/j.ajhg.2013.02.005
↑ Takizawa M, Arimori T, Taniguchi Y, Kitago Y, Yamashita E, Takagi J, Sekiguchi K. Mechanistic basis for the recognition of laminin-511 by alpha6beta1 integrin. Sci Adv. 2017 Sep 1;3(9):e1701497. doi: 10.1126/sciadv.1701497. eCollection 2017 , Sep. PMID:28879238 doi:http://dx.doi.org/10.1126/sciadv.1701497

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5xau"

@@ Line 1: / Line 1: @@
 ==Crystal structure of integrin binding fragment of laminin-511==
-<StructureSection load='5xau' size='340' side='right' caption='[[5xau]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='5xau' size='340' side='right'caption='[[5xau]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5xau]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XAU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XAU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5xau]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XAU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5XAU FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+</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>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5xau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xau OCA], [http://pdbe.org/5xau PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xau RCSB], [http://www.ebi.ac.uk/pdbsum/5xau PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xau ProSAT]</span></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LAMA5, KIAA0533, KIAA1907 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), LAMB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), LAMC1, LAMB2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5xau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xau OCA], [http://pdbe.org/5xau PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xau RCSB], [http://www.ebi.ac.uk/pdbsum/5xau PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xau ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 20: / Line 21: @@
 </div>
 <div class="pdbe-citations 5xau" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Laminin|Laminin]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Arimori, T]]
 [[Category: Kitago, Y]]

5xau

From Proteopedia

Current revision

Crystal structure of integrin binding fragment of laminin-511

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox