Related ArticlesNMR studies of caldesmon-calmodulin interactions.
Biochemistry. 1997 Mar 11;36(10):2817-25
Authors: Zhou N, Yuan T, Mak AS, Vogel HJ
The binding of the calcium-regulatory protein calmodulin (CaM) to caldesmon (CaD) contributes to the regulation of smooth muscle contraction. Two regions of caldesmon have been identified as putative calmodulin-binding domains. We have earlier reported on the binding of one of these domains to calmodulin (Zhang & Vogel (1994) Biochemistry 33, 1163-1171). Here we have studied the binding of CaM to synthetic peptides of CaD which contain: (1) both the first and second CaM-binding domains; (2) the second CaM-binding domain; and (3) the sequence between the first and second CaM-binding domains. Two-dimensional transferred nuclear Overhauser enhancement proton NMR measurements as well as circular dichroism studies of a 22-residue peptide NKETAGLKVGVSSRINEWLTK, which contains the second CaM-binding domain, show that only the C-terminal half of the peptide becomes alpha-helical upon binding to CaM. Somewhat surprisingly, the shorter 9-residue peptide SRINEWLTK was sufficient to form a 1:1 complex with CaM; this peptide appears to bind as a 3(10)-helix. Proton-carbon-13 correlation NMR titration studies with specifically labeled [methyl-13C]methionine CaM were used to study the participation of the hydrophobic regions in both domains of the dumbbell shaped CaM in peptide binding. Binding of a 54-residue CaD peptide containing both CaM-binding domains affects all the 8 Met residues in the two hydrophobic domains of CaM (only Met 76 in the linker region of CaM is not involved), while binding of the second CaM-binding domain of CaD influences principally Met 51, 71, and Met 124, 144. Simultaneous binding to CaM of two peptides comprising the first and the second CaM-binding domains also caused changes to all Met residues except Met 76. Taken together, these data demonstrate that both CaM-binding domains of CaD can bind simultaneously to the two hydrophobic regions of CaM.
[NMR paper] Metal ion binding to calmodulin: NMR and fluorescence studies.
Metal ion binding to calmodulin: NMR and fluorescence studies.
Related Articles Metal ion binding to calmodulin: NMR and fluorescence studies.
Biometals. 1998 Sep;11(3):213-22
Authors: Ouyang H, Vogel HJ
Calmodulin is an important second messenger protein which is involved in a large variety of cellular pathways. Calmodulin is sensitive to fluctuations in the intracellular Ca2+ levels and is activated by the binding of four Ca2+ ions. In spite of the important role it plays in signal transduction pathways, it shows a surprisingly broad...
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[NMR paper] Melatonin and serotonin interactions with calmodulin: NMR, spectroscopic and biochemi
Melatonin and serotonin interactions with calmodulin: NMR, spectroscopic and biochemical studies.
Related Articles Melatonin and serotonin interactions with calmodulin: NMR, spectroscopic and biochemical studies.
Biochim Biophys Acta. 1998 Mar 3;1383(1):37-47
Authors: Ouyang H, Vogel HJ
It has been reported that the hormone melatonin binds tightly to the ubiquitous calcium-regulatory protein, calmodulin (CaM) with a Kd value around 0.1 nM . Normally CaM only binds to target proteins and various 20-residue synthetic peptides encompassing the...
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[NMR paper] NMR studies of caldesmon-calmodulin interactions.
NMR studies of caldesmon-calmodulin interactions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR studies of caldesmon-calmodulin interactions.
Biochemistry. 1997 Mar 11;36(10):2817-25
Authors: Zhou N, Yuan T, Mak AS, Vogel HJ
The binding of the calcium-regulatory protein calmodulin (CaM) to caldesmon (CaD) contributes to the regulation of smooth muscle contraction. Two regions of caldesmon have been identified as putative calmodulin-binding domains. We have earlier reported on the...
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08-22-2010 03:03 PM
[NMR paper] Protein engineering and NMR studies of calmodulin.
Protein engineering and NMR studies of calmodulin.
Related Articles Protein engineering and NMR studies of calmodulin.
Mol Cell Biochem. 1995 Aug-Sep;149-150:3-15
Authors: Vogel HJ, Zhang M
The calcium regulatory protein calmodulin (CaM) plays a role as an on-off switch in the activation of many enzymes and proteins. CaM has a dumbbell shaped structure with two folded domains, which are connected by a flexible linker in solution. The calmodulin-binding domains of the target proteins are contained in 20 residue long amino acid sequences, that...
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[NMR paper] Two-dimensional NMR studies of selenomethionyl calmodulin.
Two-dimensional NMR studies of selenomethionyl calmodulin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Two-dimensional NMR studies of selenomethionyl calmodulin.
J Mol Biol. 1994 Jun 17;239(4):545-54
Authors: Zhang M, Vogel HJ
Calmodulin (CaM) is a ubiquitous calcium regulatory protein that can interact with almost 30 different target proteins. The majority of the CaM-binding domains of the target proteins are believed to interact with two hydrophobic surfaces on...
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08-22-2010 03:33 AM
[NMR paper] Two-dimensional NMR studies of selenomethionyl calmodulin.
Two-dimensional NMR studies of selenomethionyl calmodulin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Two-dimensional NMR studies of selenomethionyl calmodulin.
J Mol Biol. 1994 Jun 17;239(4):545-54
Authors: Zhang M, Vogel HJ
Calmodulin (CaM) is a ubiquitous calcium regulatory protein that can interact with almost 30 different target proteins. The majority of the CaM-binding domains of the target proteins are believed to interact with two hydrophobic surfaces on...
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08-22-2010 03:33 AM
[NMR paper] Interaction of calmodulin with phospholamban and caldesmon: comparative studies by 1H
Interaction of calmodulin with phospholamban and caldesmon: comparative studies by 1H-NMR spectroscopy.
Related Articles Interaction of calmodulin with phospholamban and caldesmon: comparative studies by 1H-NMR spectroscopy.
Biochim Biophys Acta. 1992 Nov 10;1160(1):22-34
Authors: Gao Y, Levine BA, Mornet D, Slatter DA, Strasburg GM
In order to identify comparative aspects of the interaction of calmodulin with its target proteins, proton magnetic-resonance studies of complex formation between calmodulin and defined segments of phospholamban...