4f7h: Difference between revisions

Latest revision as of 15:18, 14 March 2024

The crystal structure of kindlin-2 pleckstrin homology domain in free form

Structural highlights

4f7h 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 1.9Å
Ligands:	SRT
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FERM2_HUMAN Scaffolding protein that enhances integrin activation mediated by TLN1 and/or TLN2, but activates integrins only weakly by itself. Binds to membranes enriched in phosphoinositides. Enhances integrin-mediated cell adhesion onto the extracellular matrix and cell spreading; this requires both its ability to interact with integrins and with phospholipid membranes. Required for the assembly of focal adhesions. Participates in the connection between extracellular matrix adhesion sites and the actin cytoskeleton and also in the orchestration of actin assembly and cell shape modulation. Recruits FBLIM1 to focal adhesions. Plays a role in the TGFB1 and integrin signaling pathways. Stabilizes active CTNNB1 and plays a role in the regulation of transcription mediated by CTNNB1 and TCF7L2/TCF4 and in Wnt signaling.^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

References

↑ Tu Y, Wu S, Shi X, Chen K, Wu C. Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation. Cell. 2003 Apr 4;113(1):37-47. PMID:12679033
↑ Ma YQ, Qin J, Wu C, Plow EF. Kindlin-2 (Mig-2): a co-activator of beta3 integrins. J Cell Biol. 2008 May 5;181(3):439-46. doi: 10.1083/jcb.200710196. PMID:18458155 doi:https://dx.doi.org/10.1083/jcb.200710196
↑ Qu H, Tu Y, Shi X, Larjava H, Saleem MA, Shattil SJ, Fukuda K, Qin J, Kretzler M, Wu C. Kindlin-2 regulates podocyte adhesion and fibronectin matrix deposition through interactions with phosphoinositides and integrins. J Cell Sci. 2011 Mar 15;124(Pt 6):879-91. doi: 10.1242/jcs.076976. Epub 2011 Feb , 15. PMID:21325030 doi:https://dx.doi.org/10.1242/jcs.076976
↑ Yu Y, Wu J, Wang Y, Zhao T, Ma B, Liu Y, Fang W, Zhu WG, Zhang H. Kindlin 2 forms a transcriptional complex with beta-catenin and TCF4 to enhance Wnt signalling. EMBO Rep. 2012 Aug;13(8):750-8. doi: 10.1038/embor.2012.88. Epub 2012 Jun 15. PMID:22699938 doi:https://dx.doi.org/10.1038/embor.2012.88
↑ Liu J, Fukuda K, Xu Z, Ma YQ, Hirbawi J, Mao X, Wu C, Plow EF, Qin J. Structural basis of phosphoinositide binding to kindlin-2 protein pleckstrin homology domain in regulating integrin activation. J Biol Chem. 2011 Dec 16;286(50):43334-42. Epub 2011 Oct 26. PMID:22030399 doi:10.1074/jbc.M111.295352
↑ Perera HD, Ma YQ, Yang J, Hirbawi J, Plow EF, Qin J. Membrane Binding of the N-Terminal Ubiquitin-Like Domain of kindlin-2 Is Crucial for Its Regulation of Integrin Activation. Structure. 2011 Nov 9;19(11):1664-71. PMID:22078565 doi:10.1016/j.str.2011.08.012

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Tu Y, Wu S, Shi X, Chen K, Wu C. Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation. Cell. 2003 Apr 4;113(1):37-47. PMID:12679033

[2] Ma YQ, Qin J, Wu C, Plow EF. Kindlin-2 (Mig-2): a co-activator of beta3 integrins. J Cell Biol. 2008 May 5;181(3):439-46. doi: 10.1083/jcb.200710196. PMID:18458155 doi:https://dx.doi.org/10.1083/jcb.200710196

[3] Qu H, Tu Y, Shi X, Larjava H, Saleem MA, Shattil SJ, Fukuda K, Qin J, Kretzler M, Wu C. Kindlin-2 regulates podocyte adhesion and fibronectin matrix deposition through interactions with phosphoinositides and integrins. J Cell Sci. 2011 Mar 15;124(Pt 6):879-91. doi: 10.1242/jcs.076976. Epub 2011 Feb , 15. PMID:21325030 doi:https://dx.doi.org/10.1242/jcs.076976

[4] Yu Y, Wu J, Wang Y, Zhao T, Ma B, Liu Y, Fang W, Zhu WG, Zhang H. Kindlin 2 forms a transcriptional complex with beta-catenin and TCF4 to enhance Wnt signalling. EMBO Rep. 2012 Aug;13(8):750-8. doi: 10.1038/embor.2012.88. Epub 2012 Jun 15. PMID:22699938 doi:https://dx.doi.org/10.1038/embor.2012.88

[5] Liu J, Fukuda K, Xu Z, Ma YQ, Hirbawi J, Mao X, Wu C, Plow EF, Qin J. Structural basis of phosphoinositide binding to kindlin-2 protein pleckstrin homology domain in regulating integrin activation. J Biol Chem. 2011 Dec 16;286(50):43334-42. Epub 2011 Oct 26. PMID:22030399 doi:10.1074/jbc.M111.295352

[6] Perera HD, Ma YQ, Yang J, Hirbawi J, Plow EF, Qin J. Membrane Binding of the N-Terminal Ubiquitin-Like Domain of kindlin-2 Is Crucial for Its Regulation of Integrin Activation. Structure. 2011 Nov 9;19(11):1664-71. PMID:22078565 doi:10.1016/j.str.2011.08.012

[1]

[2]

[3]

[4]

[5]

[6]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4f7h is ON HOLD
+==The crystal structure of kindlin-2 pleckstrin homology domain in free form==
+<StructureSection load='4f7h' size='340' side='right'caption='[[4f7h]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-Authors: Liu, Y., Zhu, Y., Qin, J., Ye, S., Zhang, R.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4f7h]] 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=4F7H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F7H FirstGlance]. <br>
-Description: The crystal structure of kindlin-2 pleckstrin homology domain in free form
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SRT:S,R+MESO-TARTARIC+ACID'>SRT</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=4f7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f7h OCA], [https://pdbe.org/4f7h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f7h RCSB], [https://www.ebi.ac.uk/pdbsum/4f7h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f7h ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FERM2_HUMAN FERM2_HUMAN] Scaffolding protein that enhances integrin activation mediated by TLN1 and/or TLN2, but activates integrins only weakly by itself. Binds to membranes enriched in phosphoinositides. Enhances integrin-mediated cell adhesion onto the extracellular matrix and cell spreading; this requires both its ability to interact with integrins and with phospholipid membranes. Required for the assembly of focal adhesions. Participates in the connection between extracellular matrix adhesion sites and the actin cytoskeleton and also in the orchestration of actin assembly and cell shape modulation. Recruits FBLIM1 to focal adhesions. Plays a role in the TGFB1 and integrin signaling pathways. Stabilizes active CTNNB1 and plays a role in the regulation of transcription mediated by CTNNB1 and TCF7L2/TCF4 and in Wnt signaling.<ref>PMID:12679033</ref> <ref>PMID:18458155</ref> <ref>PMID:21325030</ref> <ref>PMID:22699938</ref> <ref>PMID:22030399</ref> <ref>PMID:22078565</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Liu Y]]
+[[Category: Qin J]]
+[[Category: Ye S]]
+[[Category: Zhang R]]
+[[Category: Zhu Y]]

4f7h: Difference between revisions

Latest revision as of 15:18, 14 March 2024

The crystal structure of kindlin-2 pleckstrin homology domain in free form

Structural highlights

Function

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools