Related ArticlesProtein 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 share no obvious amino acid sequence homology. In this contribution, we discuss the features of CaM, which allow it to be rather promiscuous, and bind effectively to all these distinct domains. In particular, we describe the role of the methionine-rich hydrophobic surfaces of the protein in providing a malleable and sticky surface for binding many hydrophobic peptides. The enzyme activation properties of various Met --> Leu mutants of CaM are discussed. In addition, the role of the flexible linker region that connects the two domains is also analyzed. Finally, we describe various NMR and spectroscopic experiments that aid in determining the CaM-bound structures of synthetic peptides containing various CaM-binding domains. All structures analyzed to date are alpha-helical when bound to CaM, and they interact with CaM only through amino acid sidechains. This form of protein-protein interaction is rather unique, and may contribute to CaM's capacity to bind effectively to such a wide range of distinct partners.
NMR, biophysical and biochemical studies reveal the minimal calmodulin-binding domain of the HIV-1 matrix protein.
NMR, biophysical and biochemical studies reveal the minimal calmodulin-binding domain of the HIV-1 matrix protein.
NMR, biophysical and biochemical studies reveal the minimal calmodulin-binding domain of the HIV-1 matrix protein.
J Biol Chem. 2011 Jul 28;
Authors: Samal AB, Ghanam RH, Fernandez TF, Monroe EB, Saad JS
Subcellular distribution of Calmodulin (CaM) in human immunodeficiency virus type-1 (HIV-1) infected cells is distinct from that observed in uninfected cells. CaM has been shown to interact and co-localize with the HIV-1 Gag protein...
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[NMR paper] NMR and molecular dynamics studies of the interaction of melatonin with calmodulin.
NMR and molecular dynamics studies of the interaction of melatonin with calmodulin.
Related Articles NMR and molecular dynamics studies of the interaction of melatonin with calmodulin.
Protein Sci. 2004 Nov;13(11):2925-38
Authors: Turjanski AG, Estrin DA, Rosenstein RE, McCormick JE, Martin SR, Pastore A, Biekofsky RR, Martorana V
Pineal hormone melatonin (N-acetyl-5-methoxytryptamine) is thought to modulate the calcium/calmodulin signaling pathway either by changing intracellular Ca(2+) concentration via activation of its G-protein-coupled...
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[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] 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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[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] NMR studies of the methionine methyl groups in calmodulin.
NMR studies of the methionine methyl groups in calmodulin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR studies of the methionine methyl groups in calmodulin.
FEBS Lett. 1995 Jun 12;366(2-3):104-8
Authors: Siivari K, Zhang M, Palmer AG, Vogel HJ
Calmodulin (CaM) is a ubiquitous Ca(2+)-binding protein that can regulate a wide variety of cellular events. The protein contains 9 Met out of a total of 148 amino acid residues. The binding of Ca2+ to CaM induces...
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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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[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...