1unc: Difference between revisions
New page: left|200px<br /> <applet load="1unc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1unc" /> '''SOLUTION STRUCTURE OF THE HUMAN VILLIN C-TE... |
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'''SOLUTION STRUCTURE OF THE HUMAN VILLIN C-TERMINAL HEADPIECE SUBDOMAIN'''<br /> | '''SOLUTION STRUCTURE OF THE HUMAN VILLIN C-TERMINAL HEADPIECE SUBDOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
Headpiece (HP) is a 76-residue F-actin-binding module at the C terminus of | 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. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1UNC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with ACE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1UNC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UNC OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Fant, F.]] | [[Category: Fant, F.]] | ||
[[Category: Martins, J.]] | [[Category: Martins, J.]] | ||
[[Category: Troys, M | [[Category: Troys, M Van.]] | ||
[[Category: Vanhaesebrouck, P.]] | [[Category: Vanhaesebrouck, P.]] | ||
[[Category: Vermeulen, W.]] | [[Category: Vermeulen, W.]] | ||
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[[Category: headpiece subdomain]] | [[Category: headpiece subdomain]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:26:24 2008'' | ||
Revision as of 16:26, 21 February 2008
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SOLUTION STRUCTURE OF THE HUMAN VILLIN C-TERMINAL HEADPIECE SUBDOMAIN
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Cholestasis, progressive canalicular OMIM:[193040]
About this StructureAbout this Structure
1UNC is a Single protein structure of sequence from [1] with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Thu Feb 21 15:26:24 2008