1ckk

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[[Image:1ckk.jpg|left|200px]]
[[Image:1ckk.jpg|left|200px]]
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{{Structure
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|PDB= 1ckk |SIZE=350|CAPTION= <scene name='initialview01'>1ckk</scene>
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The line below this paragraph, containing "STRUCTURE_1ckk", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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|GENE= XENOPUS LAEVIS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 Xenopus laevis])
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|DOMAIN=
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{{STRUCTURE_1ckk| PDB=1ckk | SCENE= }}
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|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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'''CALMODULIN/RAT CA2+/CALMODULIN DEPENDENT PROTEIN KINASE FRAGMENT'''
'''CALMODULIN/RAT CA2+/CALMODULIN DEPENDENT PROTEIN KINASE FRAGMENT'''
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[[Category: Swindells, M B.]]
[[Category: Swindells, M B.]]
[[Category: Tokumitsu, H.]]
[[Category: Tokumitsu, H.]]
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[[Category: calmodulin]]
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[[Category: Calmodulin]]
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[[Category: camkk]]
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[[Category: Camkk]]
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[[Category: complex (calmodulin/peptide)]]
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[[Category: Nmr]]
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[[Category: nmr]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:49:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:23:24 2008''
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Revision as of 09:49, 2 May 2008

Image:1ckk.jpg

Template:STRUCTURE 1ckk

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 Fri May 2 12:49:58 2008

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