Structure of the smooth muscle myosin light-chain kinase calmodulin-binding domain peptide bound to calmodulin

Biochemistry ◽  
1991 ◽  
Vol 30 (42) ◽  
pp. 10078-10084 ◽  
Author(s):  
Sharon M. Roth ◽  
Diane M. Schneider ◽  
Laura A. Strobel ◽  
Mark F. A. VanBerkum ◽  
Anthony R. Means ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Light Chain ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Smooth Muscle Myosin ◽  
Binding Domain ◽  
Calmodulin Binding ◽  
Domain Peptide ◽  
Muscle Myosin

Structure of the smooth muscle myosin light-chain kinase calmodulin-binding domain peptide bound to calmodulin [Erratum to document cited in CA115(19):201952d]

Biochemistry ◽  
1992 ◽  
Vol 31 (1) ◽  
pp. 316-316
Author(s):  
Sharon M. Roth ◽  
Diane M. Schneider ◽  
Laura A. Strobel ◽  
Mark F. A. VanBerkum ◽  
Anthony R. Means ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Light Chain ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Smooth Muscle Myosin ◽  
Binding Domain ◽  
Calmodulin Binding ◽  
Domain Peptide ◽  
Muscle Myosin

scholarly journals Affinity labelling of smooth-muscle myosin light-chain kinase with 5′-[p-(fluorosulphonyl)benzoyl]adenosine

1993 ◽  
Vol 296 (1) ◽  
pp. 53-58 ◽  
Author(s):  
H Komatsu ◽  
M Ikebe
Keyword(s):  
Smooth Muscle ◽  
Binding Site ◽  
Light Chain ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Smooth Muscle Myosin ◽  
Atp Binding ◽  
Atp Binding Site ◽  
Calmodulin Binding ◽  
Muscle Myosin

5′-(p-(Fluorosulphonyl)[14C]benzoyl)adenosine (FSBA) was synthesized and used as a probe to study the ATP-binding site of smooth-muscle myosin light-chain kinase (MLCK). FSBA modified both free MLCK and calmodulin/MLCK complex, resulting in inactivation of the kinase activity. Nearly complete protection of the calmodulin/MLCK complex against FSBA modification was obtained by addition of excess ATP whereas MLCK activity alone was lost in a dose-dependent manner even in the presence of excess ATP. These results suggest that FSBA modified ATP-binding sites and ATP-independent sites, and the latter sites are protected by calmodulin binding. The results also suggest that the ATP-binding site is accessible to the nucleotide substrate regardless of calmodulin binding. The FSBA-labelled MLCK was completely proteolysed by alpha-chymotrypsin, and the 14C-labelled peptides were isolated and sequenced. The sequence of the labelled peptide was Ala-Gly-X-Phe, where X is the labelled residue. The sequence was compared with the known MLCK sequence, and the labelled residue was identified as lysine-548, which is located downstream of the GXGXXG motif conserved among ATP-utilizing enzymes.

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