1m39
From Proteopedia
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| - | [[Image:1m39.gif|left|200px]] | + | [[Image:1m39.gif|left|200px]] |
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| - | '''Solution structure of the C-terminal fragment (F86-I165) of the human centrin 2 in calcium saturated form''' | + | {{Structure |
| + | |PDB= 1m39 |SIZE=350|CAPTION= <scene name='initialview01'>1m39</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= CEN2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Solution structure of the C-terminal fragment (F86-I165) of the human centrin 2 in calcium saturated form''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1M39 is a [ | + | 1M39 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=1M39 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12578356 12578356] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ef-hand]] | [[Category: ef-hand]] | ||
| - | ''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 12:38:22 2008'' |
Revision as of 10:38, 20 March 2008
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| Gene: | CEN2 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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