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| - | [[Image:1gjy.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1gjy| PDB=1gjy | SCENE= }} | | {{STRUCTURE_1gjy| PDB=1gjy | SCENE= }} |
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| - | '''THE X-RAY STRUCTURE OF THE SORCIN CALCIUM BINDING DOMAIN (SCBD) PROVIDES INSIGHT INTO THE PHOSPHORYLATION AND CALCIUM DEPENDENT PROCESSESS'''
| + | ===THE X-RAY STRUCTURE OF THE SORCIN CALCIUM BINDING DOMAIN (SCBD) PROVIDES INSIGHT INTO THE PHOSPHORYLATION AND CALCIUM DEPENDENT PROCESSESS=== |
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| - | ==Overview==
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| - | Sorcin is a 21.6 kDa calcium binding protein, expressed in a number of mammalian tissues that belongs to the small, recently identified penta-EF-hand (PEF) family. Like all members of this family, sorcin undergoes a Ca2+-dependent translocation from cytosol to membranes where it binds to target proteins. For sorcin, the targets differ in different tissues, indicating that it takes part in a number of Ca2+-regulated processes. The sorcin monomer is organized in two domains like in all PEF proteins: a flexible, hydrophobic, glycine-rich N-terminal region and a calcium binding C-terminal domain. In vitro, the PEF proteins are dimeric in their Ca2+-free form, but have a marked tendency to precipitate when bound to calcium. Stabilization of the dimeric structure is achieved by pairing of the uneven EF-hand, EF5. Sorcin can also form tetramers at acid pH.The sorcin calcium binding domain (SCBD, residues 33-198) expressed in Escherichia coli was crystallized in the Ca2+-free form. The structure was solved by molecular replacement and was refined to 2.2 A with a crystallographic R-factor of 22.4 %. Interestingly, the asymmetric unit contains two dimers.The structure of the SCBD leads to a model that explains the solution properties and describes the Ca2+-induced conformational changes. Phosphorylation studies show that the N-terminal domain hinders phosphorylation of SCBD, i.e. the rate of phosphorylation increased twofold in the absence of the N-terminal region. In addition, previous fluorescence studies indicated that hydrophobic residues are exposed to solvent upon Ca2+ binding to full-length sorcin. The model accounts for these data by proposing that Ca2+ binding weakens the interactions between the two domains and leads to their reorientation, which exposes hydrophobic regions facilitating the Ca2+-dependent binding to target proteins at or near membranes.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11922676}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11922676 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11922676}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Calcium-binding]] | | [[Category: Calcium-binding]] |
| | [[Category: Phosphorylation]] | | [[Category: Phosphorylation]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:40:16 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:24:48 2008'' |
Revision as of 02:24, 1 July 2008
Template:STRUCTURE 1gjy
THE X-RAY STRUCTURE OF THE SORCIN CALCIUM BINDING DOMAIN (SCBD) PROVIDES INSIGHT INTO THE PHOSPHORYLATION AND CALCIUM DEPENDENT PROCESSESS
Template:ABSTRACT PUBMED 11922676
About this Structure
1GJY is a Single protein structure of sequence from Cricetulus longicaudatus. Full crystallographic information is available from OCA.
Reference
The crystal structure of the sorcin calcium binding domain provides a model of Ca2+-dependent processes in the full-length protein., Ilari A, Johnson KA, Nastopoulos V, Verzili D, Zamparelli C, Colotti G, Tsernoglou D, Chiancone E, J Mol Biol. 2002 Mar 29;317(3):447-58. PMID:11922676
Page seeded by OCA on Tue Jul 1 05:24:48 2008
