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1und

From Proteopedia

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Current revision

Solution structure of the human advillin C-terminal headpiece subdomain

Structural highlights

1und is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

AVIL_HUMAN The disease is caused by variants affecting the gene represented in this entry.

Function

AVIL_HUMAN Ca(2+)-regulated actin-binding protein which plays an important role in actin bundling (PubMed:29058690). May have a unique function in the morphogenesis of neuronal cells which form ganglia. Required for SREC1-mediated regulation of neurite-like outgrowth. Plays a role in regenerative sensory axon outgrowth and remodeling processes after peripheral injury in neonates. Involved in the formation of long fine actin-containing filopodia-like structures in fibroblast. Plays a role in ciliogenesis. In podocytes, controls lamellipodia formation through the regulation of EGF-induced diacylglycerol generation by PLCE1 and ARP2/3 complex assembly (PubMed:29058690).^[1] ^[2]

Evolutionary Conservation

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

Publication Abstract from PubMed

Headpiece (HP) is a 76-residue F-actin-binding module at the C terminus of many cytoskeletal proteins. Its 35-residue C-terminal subdomain is one of the smallest known motifs capable of autonomously adopting a stable, folded structure in the absence of any disulfide bridges, metal ligands, or unnatural amino acids. We report the three-dimensional solution structures of the C-terminal headpiece subdomains of human villin (HVcHP) and human advillin (HAcHP), determined by two-dimensional 1H-NMR. They represent the second and third structures of such C-terminal headpiece subdomains to be elucidated so far. A comparison with the structure of the chicken villin C-terminal subdomain reveals a high structural conservation. Both C-terminal subdomains bind specifically to F-actin. Mutagenesis is used to demonstrate the involvement of Trp 64 in the F-actin-binding surface. The latter residue is part of a conserved structural feature, in which the surface-exposed indole ring is stacked on the proline and lysine side chain embedded in a PXWK sequence motif. On the basis of the structural and mutational data concerning Trp 64 reported here, the results of a cysteine-scanning mutagenesis study of full headpiece, and a phage display mutational study of the 69-74 fragment, we propose a modification of the model, elaborated by Vardar and coworkers, for the binding of headpiece to F-actin.

Solution structures of the C-terminal headpiece subdomains of human villin and advillin, evaluation of headpiece F-actin-binding requirements.,Vermeulen W, Vanhaesebrouck P, Van Troys M, Verschueren M, Fant F, Goethals M, Ampe C, Martins JC, Borremans FA Protein Sci. 2004 May;13(5):1276-87. PMID:15096633^[3]

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

References

↑ Kim J, Lee JE, Heynen-Genel S, Suyama E, Ono K, Lee K, Ideker T, Aza-Blanc P, Gleeson JG. Functional genomic screen for modulators of ciliogenesis and cilium length. Nature. 2010 Apr 15;464(7291):1048-51. doi: 10.1038/nature08895. PMID:20393563 doi:10.1038/nature08895
↑ Rao J, Ashraf S, Tan W, van der Ven AT, Gee HY, Braun DA, Fehér K, George SP, Esmaeilniakooshkghazi A, Choi WI, Jobst-Schwan T, Schneider R, Schmidt JM, Widmeier E, Warejko JK, Hermle T, Schapiro D, Lovric S, Shril S, Daga A, Nayir A, Shenoy M, Tse Y, Bald M, Helmchen U, Mir S, Berdeli A, Kari JA, El Desoky S, Soliman NA, Bagga A, Mane S, Jairajpuri MA, Lifton RP, Khurana S, Martins JC, Hildebrandt F. Advillin acts upstream of phospholipase C ϵ1 in steroid-resistant nephrotic syndrome. J Clin Invest. 2017 Dec 1;127(12):4257-4269. PMID:29058690 doi:10.1172/JCI94138
↑ Vermeulen W, Vanhaesebrouck P, Van Troys M, Verschueren M, Fant F, Goethals M, Ampe C, Martins JC, Borremans FA. Solution structures of the C-terminal headpiece subdomains of human villin and advillin, evaluation of headpiece F-actin-binding requirements. Protein Sci. 2004 May;13(5):1276-87. PMID:15096633 doi:10.1110/ps.03518104

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1und"

@@ Line 1: / Line 1: @@
 ==Solution structure of the human advillin C-terminal headpiece subdomain==
-<StructureSection load='1und' size='340' side='right'caption='[[1und]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
+<StructureSection load='1und' size='340' side='right'caption='[[1und]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1und]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UND OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UND FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1und]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UND OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UND FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1und FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1und OCA], [http://pdbe.org/1und PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1und RCSB], [http://www.ebi.ac.uk/pdbsum/1und PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1und ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</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=1und FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1und OCA], [https://pdbe.org/1und PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1und RCSB], [https://www.ebi.ac.uk/pdbsum/1und PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1und ProSAT]</span></td></tr>
 </table>
+== Disease ==
+[https://www.uniprot.org/uniprot/AVIL_HUMAN AVIL_HUMAN] The disease is caused by variants affecting the gene represented in this entry.
+== Function ==
+[https://www.uniprot.org/uniprot/AVIL_HUMAN AVIL_HUMAN] Ca(2+)-regulated actin-binding protein which plays an important role in actin bundling (PubMed:29058690). May have a unique function in the morphogenesis of neuronal cells which form ganglia. Required for SREC1-mediated regulation of neurite-like outgrowth. Plays a role in regenerative sensory axon outgrowth and remodeling processes after peripheral injury in neonates. Involved in the formation of long fine actin-containing filopodia-like structures in fibroblast. Plays a role in ciliogenesis. In podocytes, controls lamellipodia formation through the regulation of EGF-induced diacylglycerol generation by PLCE1 and ARP2/3 complex assembly (PubMed:29058690).<ref>PMID:20393563</ref> <ref>PMID:29058690</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 38: @@
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Ampe, C]]
+[[Category: Ampe C]]
-[[Category: Borremans, F]]
+[[Category: Borremans F]]
-[[Category: Fant, F]]
+[[Category: Fant F]]
-[[Category: Martins, J]]
+[[Category: Martins J]]
-[[Category: Troys, M Van]]
+[[Category: Van Troys M]]
-[[Category: Vanhaesebrouck, P]]
+[[Category: Vanhaesebrouck P]]
-[[Category: Vermeulen, W]]
+[[Category: Vermeulen W]]
-[[Category: Verschueren, M]]
+[[Category: Verschueren M]]
-[[Category: Actin binding]]
-[[Category: Cytoskeleton]]
-[[Category: F-actin binding]]
-[[Category: Headpiece subdomain]]

1und

From Proteopedia

Current revision

Solution structure of the human advillin C-terminal headpiece subdomain

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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