1ckk
From Proteopedia
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|PDB= 1ckk |SIZE=350|CAPTION= <scene name='initialview01'>1ckk</scene> | |PDB= 1ckk |SIZE=350|CAPTION= <scene name='initialview01'>1ckk</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= XENOPUS LAEVIS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 Xenopus laevis]) | |GENE= XENOPUS LAEVIS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 Xenopus laevis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ckk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ckk OCA], [http://www.ebi.ac.uk/pdbsum/1ckk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ckk RCSB]</span> | ||
}} | }} | ||
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[[Category: Swindells, M B.]] | [[Category: Swindells, M B.]] | ||
[[Category: Tokumitsu, H.]] | [[Category: Tokumitsu, H.]] | ||
| - | [[Category: CA]] | ||
[[Category: calmodulin]] | [[Category: calmodulin]] | ||
[[Category: camkk]] | [[Category: camkk]] | ||
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[[Category: nmr]] | [[Category: nmr]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:23:24 2008'' |
Revision as of 16:23, 30 March 2008
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| Ligands: | |||||||
| Gene: | XENOPUS LAEVIS (Xenopus laevis) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Sun Mar 30 19:23:24 2008
