1zmz
From Proteopedia
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'''Solution structure of the N-terminal domain (M1-S98) of human centrin 2''' | '''Solution structure of the N-terminal domain (M1-S98) of human centrin 2''' | ||
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[[Category: Miron, S.]] | [[Category: Miron, S.]] | ||
[[Category: Yang, A.]] | [[Category: Yang, A.]] | ||
| - | [[Category: | + | [[Category: Ca2+ binding]] |
| - | [[Category: | + | [[Category: Ef-hand domain]] |
| - | [[Category: | + | [[Category: Human centrin]] |
| - | [[Category: | + | [[Category: Self-association]] |
| - | [[Category: | + | [[Category: Solution structure]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:49:41 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 14:49, 3 May 2008
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 Page seeded by OCA on Sat May 3 17:49:41 2008
