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1zmz
From Proteopedia
(New page: 200px<br /> <applet load="1zmz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zmz" /> '''Solution structure of the N-terminal domain...) |
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| - | [[Image:1zmz.gif|left|200px]]<br /> | + | [[Image:1zmz.gif|left|200px]]<br /><applet load="1zmz" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1zmz" size=" | + | |
caption="1zmz" /> | caption="1zmz" /> | ||
'''Solution structure of the N-terminal domain (M1-S98) of human centrin 2'''<br /> | '''Solution structure of the N-terminal domain (M1-S98) of human centrin 2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Centrins are well-conserved calcium binding proteins from the EF-hand | + | Centrins are well-conserved calcium binding proteins from the EF-hand superfamily implicated in various cellular functions, such as centrosome duplication, DNA repair, and nuclear mRNA export. The intrinsic molecular flexibility and the self-association tendency make difficult the structural characterization of the integral protein. In this paper we report the solution structure, the Ca2+ binding properties, and the intermolecular interactions of the N-terminal domain of two human centrin isoforms, HsCen1 and HsCen2. In the absence of Ca2+, the N-terminal construct of HsCen2 revealed a compact core conformation including four almost antiparallel alpha-helices and a short antiparallel beta-sheet, very similar to the apo state structure of other calcium regulatory EF-hand domains. The first 25 residues show a highly irregular and dynamic structure. The three-dimensional model for the N-terminal domain of HsCen1, based on the high sequence conservation and NMR spectroscopic data, shows very close structural properties. Ca2+ titration of the apo-N-terminal domain of HsCen1 and HsCen2, monitored by NMR spectroscopy, revealed a very weak affinity (10(2)-10(3) M(-1)), suggesting that the cellular role of this domain is not calcium dependent. Isothermal calorimetric titrations showed that an 18-residue peptide, derived from the N-terminal unstructured fragment, has a significant affinity (approximately 10(5) M(-1)) for the isolated C-terminal domain, suggesting an active role in the self-assembly of centrin molecules. |
==About this Structure== | ==About this Structure== | ||
| - | 1ZMZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1ZMZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZMZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Assairi, L.]] | [[Category: Assairi, L.]] | ||
[[Category: Blouquit, Y.]] | [[Category: Blouquit, Y.]] | ||
| - | [[Category: Craescu, C | + | [[Category: Craescu, C T.]] |
[[Category: Duchambon, P.]] | [[Category: Duchambon, P.]] | ||
[[Category: Miron, S.]] | [[Category: Miron, S.]] | ||
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[[Category: human centrins; ef-hand domains; ca2+ binding; solution structure; self-associations]] | [[Category: human centrins; ef-hand domains; ca2+ binding; solution structure; self-associations]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:17:08 2008'' |
Revision as of 14:17, 21 February 2008
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Solution structure of the N-terminal domain (M1-S98) of human centrin 2
Overview
Centrins are well-conserved calcium binding proteins from the EF-hand superfamily implicated in various cellular functions, such as centrosome duplication, DNA repair, and nuclear mRNA export. The intrinsic molecular flexibility and the self-association tendency make difficult the structural characterization of the integral protein. In this paper we report the solution structure, the Ca2+ binding properties, and the intermolecular interactions of the N-terminal domain of two human centrin isoforms, HsCen1 and HsCen2. In the absence of Ca2+, the N-terminal construct of HsCen2 revealed a compact core conformation including four almost antiparallel alpha-helices and a short antiparallel beta-sheet, very similar to the apo state structure of other calcium regulatory EF-hand domains. The first 25 residues show a highly irregular and dynamic structure. The three-dimensional model for the N-terminal domain of HsCen1, based on the high sequence conservation and NMR spectroscopic data, shows very close structural properties. Ca2+ titration of the apo-N-terminal domain of HsCen1 and HsCen2, monitored by NMR spectroscopy, revealed a very weak affinity (10(2)-10(3) M(-1)), suggesting that the cellular role of this domain is not calcium dependent. Isothermal calorimetric titrations showed that an 18-residue peptide, derived from the N-terminal unstructured fragment, has a significant affinity (approximately 10(5) M(-1)) for the isolated C-terminal domain, suggesting an active role in the self-assembly of centrin molecules.
About this Structure
1ZMZ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The N-terminal domain of human centrin 2 has a closed structure, binds calcium with a very low affinity, and plays a role in the protein self-assembly., Yang A, Miron S, Duchambon P, Assairi L, Blouquit Y, Craescu CT, Biochemistry. 2006 Jan 24;45(3):880-9. PMID:16411764
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