1zmz
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(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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Revision as of 18:30, 12 November 2007
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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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