PMID- 10467092
OWN - NLM
STAT- MEDLINE
DCOM- 19990921
LR  - 20211203
IS  - 1072-8368 (Print)
IS  - 1072-8368 (Linking)
VI  - 6
IP  - 9
DP  - 1999 Sep
TI  - A novel target recognition revealed by calmodulin in complex with
      Ca2+-calmodulin-dependent kinase kinase.
PG  - 819-24
AB  - 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.
FAU - Osawa, M
AU  - Osawa M
AD  - Molecular Chemistry Research, Chemistry Laboratories, Institute for Drug
      Discovery Research, Yamanouchi Pharmaceutical Co., Ltd., Tsukuba 305-8585, Japan.
FAU - Tokumitsu, H
AU  - Tokumitsu H
FAU - Swindells, M B
AU  - Swindells MB
FAU - Kurihara, H
AU  - Kurihara H
FAU - Orita, M
AU  - Orita M
FAU - Shibanuma, T
AU  - Shibanuma T
FAU - Furuya, T
AU  - Furuya T
FAU - Ikura, M
AU  - Ikura M
LA  - eng
SI  - PDB/1CKK
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Nat Struct Biol
JT  - Nature structural biology
JID - 9421566
RN  - 0 (Calmodulin)
RN  - 0 (Peptide Fragments)
RN  - EC 2.7.11.1 (Protein Serine-Threonine Kinases)
RN  - EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinase Kinase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Amino Acid Substitution
MH  - Animals
MH  - Binding Sites
MH  - COS Cells
MH  - Calcium-Calmodulin-Dependent Protein Kinase Kinase
MH  - Calmodulin/*chemistry/genetics/*metabolism
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Nuclear Magnetic Resonance, Biomolecular
MH  - Peptide Fragments/chemistry/metabolism
MH  - Protein Binding
MH  - Protein Conformation
MH  - Protein Serine-Threonine Kinases/*chemistry/genetics/*metabolism
MH  - Protein Structure, Secondary
MH  - Rats
MH  - Sequence Alignment
MH  - Transfection
EDAT- 1999/08/31 09:00
MHDA- 2001/03/23 10:01
CRDT- 1999/08/31 09:00
PHST- 1999/08/31 09:00 [pubmed]
PHST- 2001/03/23 10:01 [medline]
PHST- 1999/08/31 09:00 [entrez]
AID - 10.1038/12271 [doi]
PST - ppublish
SO  - Nat Struct Biol. 1999 Sep;6(9):819-24. doi: 10.1038/12271.