4edm

From Proteopedia

(Difference between revisions)

Revision as of 07:06, 28 September 2022

Crystal structure of beta-parvin CH2 domain

Structural highlights

4edm is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PARVB_HUMAN] Adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases CDC42 and RAC1 by guanine exchange factors, such as ARHGEF6. Is involved in the reorganization of the actin cytoskeleton and formation of lamellipodia. Plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration.^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

beta-Parvin is a cytoplasmic adaptor protein that localizes to focal adhesions where it interacts with integrin-linked kinase and is involved in linking integrin receptors to the cytoskeleton. It has been reported that despite high sequence similarity to alpha-parvin, beta-parvin does not bind paxillin, suggesting distinct interactions and cellular functions for these two closely related parvins. Here, we reveal that beta-parvin binds directly and specifically to leucine-aspartic acid repeat (LD) motifs in paxillin via its C-terminal calponin homology (CH2) domain. We present the co-crystal structure of beta-parvin CH2 domain in complex with paxillin LD1 motif to 2.9 A resolution and find that the interaction is similar to that previously observed between alpha-parvin and paxillin LD1. We also present crystal structures of unbound beta-parvin CH2 domain at 2.1 A and 2.0 A resolution that show significant conformational flexibility in the N-terminal alpha-helix, suggesting an induced fit upon paxillin binding. We find that beta-parvin has specificity for the LD1, LD2, and LD4 motifs of paxillin, with K(D) values determined to 27, 42, and 73 mum, respectively, by surface plasmon resonance. Furthermore, we show that proper localization of beta-parvin to focal adhesions requires both the paxillin and integrin-linked kinase binding sites and that paxillin is important for early targeting of beta-parvin. These studies provide the first molecular details of beta-parvin binding to paxillin and help define the requirements for beta-parvin localization to focal adhesions.

Structural Basis for Paxillin Binding and Focal Adhesion Targeting of beta-Parvin.,Stiegler AL, Draheim KM, Li X, Chayen NE, Calderwood DA, Boggon TJ J Biol Chem. 2012 Sep 21;287(39):32566-77. Epub 2012 Aug 6. PMID:22869380^[6]

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

References

↑ Yamaji S, Suzuki A, Sugiyama Y, Koide Y, Yoshida M, Kanamori H, Mohri H, Ohno S, Ishigatsubo Y. A novel integrin-linked kinase-binding protein, affixin, is involved in the early stage of cell-substrate interaction. J Cell Biol. 2001 Jun 11;153(6):1251-64. PMID:11402068
↑ Mishima W, Suzuki A, Yamaji S, Yoshimi R, Ueda A, Kaneko T, Tanaka J, Miwa Y, Ohno S, Ishigatsubo Y. The first CH domain of affixin activates Cdc42 and Rac1 through alphaPIX, a Cdc42/Rac1-specific guanine nucleotide exchanging factor. Genes Cells. 2004 Mar;9(3):193-204. PMID:15005707
↑ Zhang Y, Chen K, Tu Y, Wu C. Distinct roles of two structurally closely related focal adhesion proteins, alpha-parvins and beta-parvins, in regulation of cell morphology and survival. J Biol Chem. 2004 Oct 1;279(40):41695-705. Epub 2004 Jul 28. PMID:15284246 doi:10.1074/jbc.M401563200
↑ Yamaji S, Suzuki A, Kanamori H, Mishima W, Yoshimi R, Takasaki H, Takabayashi M, Fujimaki K, Fujisawa S, Ohno S, Ishigatsubo Y. Affixin interacts with alpha-actinin and mediates integrin signaling for reorganization of F-actin induced by initial cell-substrate interaction. J Cell Biol. 2004 May 24;165(4):539-51. PMID:15159419 doi:10.1083/jcb.200308141
↑ Matsuda C, Kameyama K, Suzuki A, Mishima W, Yamaji S, Okamoto H, Nishino I, Hayashi YK. Affixin activates Rac1 via betaPIX in C2C12 myoblast. FEBS Lett. 2008 Apr 9;582(8):1189-96. doi: 10.1016/j.febslet.2008.01.064. Epub, 2008 Mar 4. PMID:18325335 doi:10.1016/j.febslet.2008.01.064
↑ Stiegler AL, Draheim KM, Li X, Chayen NE, Calderwood DA, Boggon TJ. Structural Basis for Paxillin Binding and Focal Adhesion Targeting of beta-Parvin. J Biol Chem. 2012 Sep 21;287(39):32566-77. Epub 2012 Aug 6. PMID:22869380 doi:10.1074/jbc.M112.367342

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Crystal structure of beta-parvin CH2 domain==
-<StructureSection load='4edm' size='340' side='right' caption='[[4edm]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='4edm' size='340' side='right'caption='[[4edm]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4edm]] is a 2 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=4EDM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EDM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4edm]] is a 2 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=4EDM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EDM FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4edl|4edl]], [[4edn|4edn]]</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=4edm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4edm OCA], [https://pdbe.org/4edm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4edm RCSB], [https://www.ebi.ac.uk/pdbsum/4edm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4edm ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PARVB, CGI-56 ([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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4edm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4edm OCA], [http://pdbe.org/4edm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4edm RCSB], [http://www.ebi.ac.uk/pdbsum/4edm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4edm ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PARVB_HUMAN PARVB_HUMAN]] Adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases CDC42 and RAC1 by guanine exchange factors, such as ARHGEF6. Is involved in the reorganization of the actin cytoskeleton and formation of lamellipodia. Plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration.<ref>PMID:11402068</ref> <ref>PMID:15005707</ref> <ref>PMID:15284246</ref> <ref>PMID:15159419</ref> <ref>PMID:18325335</ref>
+[[https://www.uniprot.org/uniprot/PARVB_HUMAN PARVB_HUMAN]] Adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases CDC42 and RAC1 by guanine exchange factors, such as ARHGEF6. Is involved in the reorganization of the actin cytoskeleton and formation of lamellipodia. Plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration.<ref>PMID:11402068</ref> <ref>PMID:15005707</ref> <ref>PMID:15284246</ref> <ref>PMID:15159419</ref> <ref>PMID:18325335</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 18: @@
 </div>
 <div class="pdbe-citations 4edm" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Parvin 3D structures|Parvin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Boggon, T J]]
+[[Category: Large Structures]]
-[[Category: Calderwood, D A]]
+[[Category: Boggon TJ]]
-[[Category: Chayen, N E]]
+[[Category: Calderwood DA]]
-[[Category: Draheim, K M]]
+[[Category: Chayen NE]]
-[[Category: Li, X]]
+[[Category: Draheim KM]]
-[[Category: Stiegler, A L]]
+[[Category: Li X]]
-[[Category: Adaptor protein]]
+[[Category: Stiegler AL]]
-[[Category: Calponin homology domain]]
-[[Category: Focal adhesion]]
-[[Category: Integrin linked kinase]]
-[[Category: Integrin signaling]]
-[[Category: Ld motif]]
-[[Category: Paxillin]]
-[[Category: Protein-protein interaction]]
-[[Category: Signaling protein]]

4edm

From Proteopedia

Revision as of 07:06, 28 September 2022

Crystal structure of beta-parvin CH2 domain

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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