1zmz
From Proteopedia
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| - | [[Image:1zmz.gif|left|200px]] | + | [[Image:1zmz.gif|left|200px]] |
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| - | '''Solution structure of the N-terminal domain (M1-S98) of human centrin 2''' | + | {{Structure |
| + | |PDB= 1zmz |SIZE=350|CAPTION= <scene name='initialview01'>1zmz</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= CETN2, CALT, CEN2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Solution structure of the N-terminal domain (M1-S98) of human centrin 2''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ZMZ is a [ | + | 1ZMZ is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16411764 16411764] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Miron, S.]] | [[Category: Miron, S.]] | ||
[[Category: Yang, A.]] | [[Category: Yang, A.]] | ||
| - | [[Category: human centrins; ef-hand domains; ca2+ binding; solution structure; self- | + | [[Category: human centrins; ef-hand domains; ca2+ binding; solution structure; self-association]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:37:29 2008'' |
Revision as of 13:37, 20 March 2008
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| Gene: | CETN2, CALT, CEN2 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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