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1m39

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[[Image:1m39.gif|left|200px]]
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|GENE= CEN2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m39 OCA], [http://www.ebi.ac.uk/pdbsum/1m39 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m39 RCSB]</span>
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'''Solution structure of the C-terminal fragment (F86-I165) of the human centrin 2 in calcium saturated form'''
'''Solution structure of the C-terminal fragment (F86-I165) of the human centrin 2 in calcium saturated form'''
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[[Category: Matei, E.]]
[[Category: Matei, E.]]
[[Category: Miron, S.]]
[[Category: Miron, S.]]
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[[Category: ef-hand]]
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[[Category: Ef-hand]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:34:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:10:44 2008''
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Revision as of 21:34, 2 May 2008

Template:STRUCTURE 1m39

Solution structure of the C-terminal fragment (F86-I165) of the human centrin 2 in calcium saturated form


Overview

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.

About this Structure

1M39 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

C-terminal half of human centrin 2 behaves like a regulatory EF-hand domain., Matei E, Miron S, Blouquit Y, Duchambon P, Durussel I, Cox JA, Craescu CT, Biochemistry. 2003 Feb 18;42(6):1439-50. PMID:12578356 Page seeded by OCA on Sat May 3 00:34:50 2008

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