1ZMZ

Solution structure of the N-terminal domain (M1-S98) of human centrin 2

Summary for 1ZMZ

• Entry DOI: 10.2210/pdb1zmz/pdb
• Descriptor: Centrin-2 (1 entity in total)
• Functional Keywords: human centrins; ef-hand domains; ca2+ binding; solution structure; self-associations, structural protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytoskeleton, centrosome, centriole: P41208
• Total number of polymer chains: 1
• Total formula weight: 11129.86

Authors

Yang, A.,Miron, S.,Duchambon, P.,Assairi, L.,Blouquit, Y.,Craescu, C.T. (deposition date: 2005-05-11, release date: 2006-04-25, Last modification date: 2024-05-22)

Primary citation

Yang, A.,Miron, S.,Duchambon, P.,Assairi, L.,Blouquit, Y.,Craescu, C.T.
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
Biochemistry, 45:880-889, 2006

PubMed Abstract: 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.

PubMed: 16411764
DOI: 10.1021/bi051397s

Experimental method

SOLUTION NMR