1ckk
From Proteopedia
(New page: 200px<br /><applet load="1ckk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ckk" /> '''CALMODULIN/RAT CA2+/CALMODULIN DEPENDENT PRO...) |
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| - | [[Image:1ckk.jpg|left|200px]]<br /><applet load="1ckk" size=" | + | [[Image:1ckk.jpg|left|200px]]<br /><applet load="1ckk" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ckk" /> | caption="1ckk" /> | ||
'''CALMODULIN/RAT CA2+/CALMODULIN DEPENDENT PROTEIN KINASE FRAGMENT'''<br /> | '''CALMODULIN/RAT CA2+/CALMODULIN DEPENDENT PROTEIN KINASE FRAGMENT'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of calcium-bound calmodulin (Ca2+/CaM) complexed with a | + | The structure of calcium-bound calmodulin (Ca2+/CaM) complexed with a 26-residue peptide, corresponding to the CaM-binding domain of rat Ca2+/CaM-dependent protein kinase kinase (CaMKK), has been determined by NMR spectroscopy. In this complex, the CaMKK peptide forms a fold comprising an alpha-helix and a hairpin-like loop whose C-terminus folds back on itself. The binding orientation of this CaMKK peptide by the two CaM domains is opposite to that observed in all other CaM-target complexes determined so far. The N- and C-terminal hydrophobic pockets of Ca2+/CaM anchor Trp 444 and Phe 459 of the CaMKK peptide, respectively. This 14-residue separation between two key hydrophobic groups is also unique among previously determined CaM complexes. The present structure represents a new and distinct class of Ca2+/CaM target recognition that may be shared by other Ca2+/CaM-stimulated proteins. |
==About this Structure== | ==About this Structure== | ||
| - | 1CKK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1CKK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CKK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Osawa, M.]] | [[Category: Osawa, M.]] | ||
[[Category: Shibanuma, T.]] | [[Category: Shibanuma, T.]] | ||
| - | [[Category: Swindells, M | + | [[Category: Swindells, M B.]] |
[[Category: Tokumitsu, H.]] | [[Category: Tokumitsu, H.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: nmr]] | [[Category: nmr]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:07:00 2008'' |
Revision as of 10:07, 21 February 2008
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CALMODULIN/RAT CA2+/CALMODULIN DEPENDENT PROTEIN KINASE FRAGMENT
Overview
The structure of calcium-bound calmodulin (Ca2+/CaM) complexed with a 26-residue peptide, corresponding to the CaM-binding domain of rat Ca2+/CaM-dependent protein kinase kinase (CaMKK), has been determined by NMR spectroscopy. In this complex, the CaMKK peptide forms a fold comprising an alpha-helix and a hairpin-like loop whose C-terminus folds back on itself. The binding orientation of this CaMKK peptide by the two CaM domains is opposite to that observed in all other CaM-target complexes determined so far. The N- and C-terminal hydrophobic pockets of Ca2+/CaM anchor Trp 444 and Phe 459 of the CaMKK peptide, respectively. This 14-residue separation between two key hydrophobic groups is also unique among previously determined CaM complexes. The present structure represents a new and distinct class of Ca2+/CaM target recognition that may be shared by other Ca2+/CaM-stimulated proteins.
About this Structure
1CKK is a Single protein structure of sequence from Rattus norvegicus and Xenopus laevis with as ligand. Full crystallographic information is available from OCA.
Reference
A novel target recognition revealed by calmodulin in complex with Ca2+-calmodulin-dependent kinase kinase., Osawa M, Tokumitsu H, Swindells MB, Kurihara H, Orita M, Shibanuma T, Furuya T, Ikura M, Nat Struct Biol. 1999 Sep;6(9):819-24. PMID:10467092
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