Related ArticlesCalcium-modulated S100 protein-phospholipid interactions. An NMR study of calbindin D9k and DPC.
Biochemistry. 2005 May 3;44(17):6502-12
Authors: Malmendal A, Vander Kooi CW, Nielsen NC, Chazin WJ
The cellular functions of several S100 proteins involve specific interactions with phospholipids and the cell membrane. The interactions between calbindin D(9k) (S100D) and the detergent dodecyl phosphocholine (DPC) were studied using NMR spectroscopy. In the absence of Ca(2+), the protein associates with DPC micelles. The micelle-associated state has intact helical secondary structures but no apparent tertiary fold. At neutral pH, Ca(2+)-loaded calbindin D(9k) does not associate with DPC micelles. However, a specific interaction is observed with individual DPC molecules at a site close to the linker between the two EF-hands. Binding to this site occurs only when Ca(2+) is bound to the protein. A reduction in pH in the absence of Ca(2+) increases the stability of the micelle-associated state. This along with the corresponding reduction in Ca(2+) affinity causes a transition to the micelle-associated state also in the presence of Ca(2+) when the pH is lowered. Site-specific analysis of the data indicates that calbindin D(9k) has a core of three tightly packed helices (A, B, and D), with a dynamic fourth helix (C) more loosely associated. Evidence is presented that the Ca(2+)-binding characteristics of the two EF-hands are distinctly different in a micelle environment. The role of calbindin D(9k) in the cell is discussed, along with the broader implications for the function of the S100 protein family.
An NMR method to study protein-protein interactions.
An NMR method to study protein-protein interactions.
An NMR method to study protein-protein interactions.
Methods Mol Biol. 2012;757:129-37
Authors: Nishida N, Shimada I
Abstract
Specific interactions between proteins are a fundamental process underlying the various biological events, such as cell-cell contacts, signal transduction, and gene expression. Therefore, the structural investigations of protein-protein interactions provide useful information for understanding these events. We describe an NMR method, termed the cross-saturation...
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Exploring NMR ensembles of calcium binding proteins: perspectives to design inhibitors of protein-protein interactions.
Exploring NMR ensembles of calcium binding proteins: perspectives to design inhibitors of protein-protein interactions.
Exploring NMR ensembles of calcium binding proteins: perspectives to design inhibitors of protein-protein interactions.
BMC Struct Biol. 2011 May 12;11(1):24
Authors: Isvoran A, Badel A, Craescu CT, Miron S, Miteva MA
ABSTRACT: BACKGROUND: Disrupting protein-protein interactions by small organic molecules is nowadays a promising strategy employed to block protein targets involved in different pathologies. However, structural...
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05-17-2011 06:21 PM
[NMR paper] Identification of Li(+) binding sites and the effect of Li(+) treatment on phospholipid composition in human neuroblastoma cells: a (7)Li and (31)P NMR study.
Identification of Li(+) binding sites and the effect of Li(+) treatment on phospholipid composition in human neuroblastoma cells: a (7)Li and (31)P NMR study.
Related Articles Identification of Li(+) binding sites and the effect of Li(+) treatment on phospholipid composition in human neuroblastoma cells: a (7)Li and (31)P NMR study.
Biochim Biophys Acta. 2005 Sep 25;1741(3):339-49
Authors: Layden BT, Abukhdeir AM, Malarkey C, Oriti LA, Salah W, Stigler C, Geraldes CF, Mota de Freitas D
Li(+) binding in subcellular fractions of human...
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12-01-2010 06:56 PM
[NMR paper] A 15N NMR mobility study on the dicalcium P43M calbindin D9k and its mono-La3+-substi
A 15N NMR mobility study on the dicalcium P43M calbindin D9k and its mono-La3+-substituted form.
Related Articles A 15N NMR mobility study on the dicalcium P43M calbindin D9k and its mono-La3+-substituted form.
Biochemistry. 2002 Apr 23;41(16):5104-11
Authors: Bertini I, Carrano CJ, Luchinat C, Piccioli M, Poggi L
Calbindin D(9k) is a dicalcium binding protein consisting of two helix-loop-helix EF-hand motifs joined together by a flexible linker region where one metal ion can bind to each of the two loops. A proline residue at position 43 in...
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11-24-2010 08:49 PM
[NMR paper] The dimerization stability of the HLH-LZ transcription protein family is modulated by
The dimerization stability of the HLH-LZ transcription protein family is modulated by the leucine zippers: a CD and NMR study of TFEB and c-Myc.
Related Articles The dimerization stability of the HLH-LZ transcription protein family is modulated by the leucine zippers: a CD and NMR study of TFEB and c-Myc.
Biochemistry. 1994 Sep 20;33(37):11296-306
Authors: Muhle-Goll C, Gibson T, Schuck P, Schubert D, Nalis D, Nilges M, Pastore A
In the HLH-LZ protein family, the helix-loop-helix DNA-binding dimerization domain is followed in the sequence by a...
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08-22-2010 03:29 AM
[NMR paper] Backbone dynamics of calcium-loaded calbindin D9k studied by two-dimensional proton-d
Backbone dynamics of calcium-loaded calbindin D9k studied by two-dimensional proton-detected 15N NMR spectroscopy.
Related Articles Backbone dynamics of calcium-loaded calbindin D9k studied by two-dimensional proton-detected 15N NMR spectroscopy.
Biochemistry. 1992 May 26;31(20):4856-66
Authors: Kördel J, Skelton NJ, Akke M, Palmer AG, Chazin WJ
Backbone dynamics of calcium-loaded calbindin D9k have been investigated by two-dimensional proton-detected heteronuclear nuclear magnetic resonance spectroscopy, using a uniformly 15N enriched...
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08-21-2010 11:41 PM
[NMR paper] 19F-NMR study of the effect of lead on intracellular free calcium in human platelets.
19F-NMR study of the effect of lead on intracellular free calcium in human platelets.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 19F-NMR study of the effect of lead on intracellular free calcium in human platelets.
Biochim Biophys Acta. 1991 May 17;1092(3):341-6
Authors: Dowd TL, Gupta RK
Lead has been shown to affect calcium homeostasis. However, there is no prior evidence to indicate an effect of low concentrations of lead in the environment (approximately 1...
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08-21-2010 11:16 PM
Postdoctoral position to study Protein-Protein Interactions and their role in Mechanisms of Signal Transduction using protein solution NMR/x-ray crystallography
Spincore.com are advertising a postdoc NMR position. It sounds pretty interesting.
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Postdoctoral position to study Protein-Protein Interactions and their role in Mechanisms of Signal Transduction using protein solution NMR /x-ray crystallography
Case Medical School, Cleveland, Ohio, USA
How are signaling events transmitted from one protein to another? To answer this question we are looking to add a postdoctoral co-workers to our interdisciplinary team. Our interest is to understand protein-protein interactions, protein structure and dynamics in the context of cell signaling...
Calcium-modulated S100 protein-phospholipid interactions. An NMR study of calbindin D
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