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C-Terminal Half of Human Centrin 2 Behaves like a Regulatory EF-Hand Domain
- Source :
- Biochemistry. 42:1439-1450
- Publication Year :
- 2003
- Publisher :
- American Chemical Society (ACS), 2003.
-
Abstract
- Human centrin 2 (HsCen2) is an EF-hand protein that plays a critical role in the centrosome duplication and separation during cell division. We studied the structural and Ca(2+)-binding properties of two C-terminal fragments of this protein: SC-HsCen2 (T94-Y172), covering two EF-hands, and LC-HsCen2 (M84-Y172), having 10 additional residues. Both fragments are highly disordered in the apo state but become better structured (although not conformationally homogeneous) in the presence of Ca(2+) and depending on the nature of the cations (K(+) or Na(+)) in the buffer. Only the longer C-terminal domain, in the Ca(2+)-saturated state and in the presence of Na(+) ions, was amenable to structure determination by nuclear magnetic resonance. The solution structure of LC-HsCen2 reveals an open two EF-hand structure, similar to the conformation of related Ca(2+)-saturated regulatory domains. Unexpectedly, the N-terminal helix segment (F86-T94) lies over the exposed hydrophobic cavity. This unusual intramolecular interaction increases considerably the Ca(2+) affinity and constitutes a useful model for the target binding.
- Subjects :
- Protein Conformation
Stereochemistry
Molecular Sequence Data
Cell Cycle Proteins
Plasma protein binding
Biology
Crystallography, X-Ray
Biochemistry
Protein structure
Calcium-binding protein
Animals
Humans
Centrosome duplication
Amino Acid Sequence
EF Hand Motifs
Nuclear Magnetic Resonance, Biomolecular
Peptide sequence
Sequence Homology, Amino Acid
EF hand
Calcium-Binding Proteins
Melitten
Peptide Fragments
Protein Structure, Tertiary
Crystallography
Spectrometry, Fluorescence
Centrin
Helix
Thermodynamics
Calcium
Sequence Alignment
Chlamydomonas reinhardtii
Protein Binding
Subjects
Details
- ISSN :
- 15204995 and 00062960
- Volume :
- 42
- Database :
- OpenAIRE
- Journal :
- Biochemistry
- Accession number :
- edsair.doi.dedup.....882f2177056ffef12832c99ccb0a56d2
- Full Text :
- https://doi.org/10.1021/bi0269714