2e6w
From Proteopedia
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|PDB= 2e6w |SIZE=350|CAPTION= <scene name='initialview01'>2e6w</scene> | |PDB= 2e6w |SIZE=350|CAPTION= <scene name='initialview01'>2e6w</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= DREAM, KCHIP3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= DREAM, KCHIP3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2e6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e6w OCA], [http://www.ebi.ac.uk/pdbsum/2e6w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2e6w RCSB]</span> | ||
}} | }} | ||
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[[Category: Sun, C.]] | [[Category: Sun, C.]] | ||
[[Category: Yu, L.]] | [[Category: Yu, L.]] | ||
| - | [[Category: CA]] | ||
[[Category: calcium-bound form]] | [[Category: calcium-bound form]] | ||
[[Category: metal binding protein]] | [[Category: metal binding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:44:40 2008'' |
Revision as of 23:44, 30 March 2008
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| Ligands: | |||||||
| Gene: | DREAM, KCHIP3 (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure and calcium binding properties of EF-hands 3 and 4 of calsenilin
Overview
Calsenilin is a member of the recoverin branch of the EF-hand superfamily that is reported to interact with presenilins, regulate prodynorphin gene expression, modulate voltage-gated Kv4 potassium channel function, and bind to neurotoxins. Calsenilin is a Ca+2-binding protein and plays an important role in calcium signaling. Despite its importance in numerous neurological functions, the structure of this protein has not been reported. In the absence of Ca+2, the protein has limited spectral resolution that increases upon the addition of Ca+2. Here, we describe the three-dimensional solution structure of EF-hands 3 and 4 of calsenilin in the Ca+2-bound form. The Ca+2-bound structure consists of five alpha-helices and one two-stranded antiparallel beta-sheet. The long loop that connects EF hands 3 and 4 is highly disordered in solution. In addition to its structural effects, Ca+2 binding also increases the protein's propensity to dimerize. These changes in structure and oligomerization state induced upon Ca+2 binding may play important roles in molecular recognition during calcium signaling.
About this Structure
2E6W is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure and calcium-binding properties of EF-hands 3 and 4 of calsenilin., Yu L, Sun C, Mendoza R, Wang J, Matayoshi ED, Hebert E, Pereda-Lopez A, Hajduk PJ, Olejniczak ET, Protein Sci. 2007 Nov;16(11):2502-9. PMID:17962406
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