1oqp
From Proteopedia
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| - | [[Image:1oqp.gif|left|200px]] | + | [[Image:1oqp.gif|left|200px]] |
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| - | '''STRUCTURE OF THE CA2+/C-TERMINAL DOMAIN OF CALTRACTIN IN COMPLEX WITH THE CDC31P-BINDING DOMAIN FROM KAR1P''' | + | {{Structure |
| + | |PDB= 1oqp |SIZE=350|CAPTION= <scene name='initialview01'>1oqp</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''STRUCTURE OF THE CA2+/C-TERMINAL DOMAIN OF CALTRACTIN IN COMPLEX WITH THE CDC31P-BINDING DOMAIN FROM KAR1P''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OQP is a [ | + | 1OQP is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OQP OCA]. |
==Reference== | ==Reference== | ||
| - | Unique features in the C-terminal domain provide caltractin with target specificity., Hu H, Chazin WJ, J Mol Biol. 2003 Jul 11;330(3):473-84. PMID:[http:// | + | Unique features in the C-terminal domain provide caltractin with target specificity., Hu H, Chazin WJ, J Mol Biol. 2003 Jul 11;330(3):473-84. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12842464 12842464] |
[[Category: Chlamydomonas reinhardtii]] | [[Category: Chlamydomonas reinhardtii]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: protein-peptide complex]] | [[Category: protein-peptide complex]] | ||
| - | ''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 13:14:20 2008'' |
Revision as of 11:14, 20 March 2008
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STRUCTURE OF THE CA2+/C-TERMINAL DOMAIN OF CALTRACTIN IN COMPLEX WITH THE CDC31P-BINDING DOMAIN FROM KAR1P
Overview
Caltractin (centrin) is a member of the calmodulin (CaM) superfamily of EF-hand calcium-binding proteins. It is an essential component of the centrosomal structures in a wide range of organisms. Caltractin and calmodulin apparently function in distinct calcium signaling pathways despite substantial sequence similarity. In an effort to understand the structural basis for such differences, the high-resolution three-dimensional solution structure of the complex between the Ca(2+)-activated C-terminal domain of Chlamydomonas reinhardtii caltractin (CRC-C) and a 19 residue peptide fragment comprising the putative cdc31p-binding region of Kar1p (K(19)) has been determined by multi-dimensional heteronuclear NMR spectroscopy. Formation of the complex is calcium-dependent and is stabilized by extensive interactions between CRC-C and three key hydrophobic anchors (Trp10, Leu13 and Leu14) in the peptide as well as favorable electrostatic interactions at the protein-peptide interface. In-depth comparisons have been made to the structure of the complex of Ca(2+)-activated calmodulin and R(20), the CaM-binding domain of smooth muscle myosin light-chain kinase. Although the overall structures of CRC and CaM domains in their respective complexes are very similar, differences in critical regions in the sequences of these proteins and their targets lead to clear differences in the complementarity of their respective binding surfaces. These subtle differences reveal the structural basis for the Ca(2+)-dependent regulation of distinct cellular signaling events by CRC and CaM.
About this Structure
1OQP is a Protein complex structure of sequences from Chlamydomonas reinhardtii. Full crystallographic information is available from OCA.
Reference
Unique features in the C-terminal domain provide caltractin with target specificity., Hu H, Chazin WJ, J Mol Biol. 2003 Jul 11;330(3):473-84. PMID:12842464
Page seeded by OCA on Thu Mar 20 13:14:20 2008
