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4u7l

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LRIG1 extracellular domain: Structure and Function Analysis

Structural highlights

4u7l is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LRIG1_HUMAN Acts as a feedback negative regulator of signaling by receptor tyrosine kinases, through a mechanism that involves enhancement of receptor ubiquitination and accelerated intracellular degradation.^[1]

Publication Abstract from PubMed

We have expressed and purified three soluble fragments of the human LRIG1-ECD (extracellular domain): the LRIG1-LRR (leucine-rich repeat) domain, the LRIG1-3Ig (immunoglobulin-like) domain, and the LRIG1-LRR-1Ig fragment using baculovirus vectors in insect cells. The two LRIG1 domains crystallised so that we have been able to determine the three-dimensional structures at 2.3A resolution. We developed a three-dimensional structure for the LRIG1-ECD using homology modelling based on the LINGO-1 structure. The LRIG1-LRR domain and the LRIG1-LRR-1Ig fragment are monomers in solution, whereas the LRIG1-3Ig domain appears to be dimeric. We could not detect any binding of the LRIG1 domains or the LRIG1-LRR-1Ig fragment to the EGF receptor (EGFR), either in solution using biosensor analysis or when the EGFR was expressed on the cell surface. The FLAG-tagged LRIG1-LRR-1Ig fragment binds weakly to colon cancer cells regardless of the presence of EGFRs. Similarly, neither the soluble LRIG1-LRR nor the LRIG1-3Ig domains nor the full-length LRIG1 co-expressed in HEK293 cells inhibited ligand-stimulated activation of cell-surface EGFR.

LRIG1 Extracellular Domain: Structure and Function Analysis.,Xu Y, Soo P, Walker F, Zhang HH, Redpath N, Tan CW, Nicola NA, Adams TE, Garrett TP, Zhang JG, Burgess AW J Mol Biol. 2015 Mar 9. pii: S0022-2836(15)00173-4. doi:, 10.1016/j.jmb.2015.03.001. PMID:25765764^[2]

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

References

↑ Gur G, Rubin C, Katz M, Amit I, Citri A, Nilsson J, Amariglio N, Henriksson R, Rechavi G, Hedman H, Wides R, Yarden Y. LRIG1 restricts growth factor signaling by enhancing receptor ubiquitylation and degradation. EMBO J. 2004 Aug 18;23(16):3270-81. Epub 2004 Jul 29. PMID:15282549 doi:http://dx.doi.org/10.1038/sj.emboj.7600342
↑ Xu Y, Soo P, Walker F, Zhang HH, Redpath N, Tan CW, Nicola NA, Adams TE, Garrett TP, Zhang JG, Burgess AW. LRIG1 Extracellular Domain: Structure and Function Analysis. J Mol Biol. 2015 Mar 9. pii: S0022-2836(15)00173-4. doi:, 10.1016/j.jmb.2015.03.001. PMID:25765764 doi:http://dx.doi.org/10.1016/j.jmb.2015.03.001

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4u7l"

Categories: Homo sapiens | Large Structures | Xu Y

@@ Line 1: / Line 1: @@
 ==LRIG1 extracellular domain: Structure and Function Analysis==
-<StructureSection load='4u7l' size='340' side='right' caption='[[4u7l]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='4u7l' size='340' side='right'caption='[[4u7l]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4u7l]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U7L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U7L FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4u7l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U7L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U7L FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.3&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4u7m|4u7m]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=4u7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u7l OCA], [http://pdbe.org/4u7l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4u7l RCSB], [http://www.ebi.ac.uk/pdbsum/4u7l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4u7l 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=4u7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u7l OCA], [https://pdbe.org/4u7l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u7l RCSB], [https://www.ebi.ac.uk/pdbsum/4u7l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u7l ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/LRIG1_HUMAN LRIG1_HUMAN]] Acts as a feedback negative regulator of signaling by receptor tyrosine kinases, through a mechanism that involves enhancement of receptor ubiquitination and accelerated intracellular degradation.<ref>PMID:15282549</ref>
+[https://www.uniprot.org/uniprot/LRIG1_HUMAN LRIG1_HUMAN] Acts as a feedback negative regulator of signaling by receptor tyrosine kinases, through a mechanism that involves enhancement of receptor ubiquitination and accelerated intracellular degradation.<ref>PMID:15282549</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Xu, Y]]
+[[Category: Homo sapiens]]
-[[Category: Egfr inhibition]]
+[[Category: Large Structures]]
-[[Category: Signaling protein]]
+[[Category: Xu Y]]
-[[Category: Stem cell marker]]

4u7l

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Current revision

LRIG1 extracellular domain: Structure and Function Analysis

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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