The structure of monomeric human chemokine IL-8 (residues 1â??66) was determined in aqueous solution by NMR spectroscopy. The structure of the monomer is similar to that of each subunit in the dimeric full-length protein (residues 1â??72), with the main differences being the location of the N-loop (residues 10â??22) relative to the C-terminal α-helix and the position of the side chain of phenylalanine 65 near the truncated dimerization interface (residues 67â??72). NMR was used to analyze the interactions of monomeric IL-8 (1â??66) with ND-CXCR1 (residues 1â??38), a soluble polypeptide corresponding to the N-terminal portion of the ligand binding site (Binding Site-I) of the chemokine receptor CXCR1 in aqueous solution, and with 1TM-CXCR1 (residues 1â??72), a membrane-associated polypeptide that includes the same N-terminal portion of the binding site, the first trans-membrane helix, and the first intracellular loop of the receptor in nanodiscs. The presence of neither the first transmembrane helix of the receptor nor the lipid bilayer significantly affected the interactions of IL-8 with Binding Site-I of CXCR1.
[NMR paper] Identification of the Glycosaminoglycan Binding Site of Interleukin-10 by NMR Spectroscopy.
Identification of the Glycosaminoglycan Binding Site of Interleukin-10 by NMR Spectroscopy.
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J Biol Chem. 2015 Dec 16;
Authors: Künze G, Köhling S, Vogel A, Rademann J, Huster D
Abstract
The biological function of interleukin-10 (IL-10), a pleiotropic cytokine with an essential role in inflammatory processes, is known to be affected by glycosaminoglycans (GAGs). GAGs are highly negatively charged polysaccharides and...
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Solution NMR characterization of WT CXCL8 monomer and dimer binding to CXCR1 N-terminal domain
Solution NMR characterization of WT CXCL8 monomer and dimer binding to CXCR1 N-terminal domain
Abstract
Chemokine CXCL8 and its receptor CXCR1 are key mediators in combating infection and have also been implicated in the pathophysiology of various diseases including chronic obstructive pulmonary disease (COPD) and cancer. CXCL8 exists as monomers and dimers but monomer alone binds CXCR1 with high affinity. CXCL8 function involves binding two distinct CXCR1 sites – the N-terminal domain (Site-I) and the extracellular/transmembrane domain (Site-II). Therefore, higher monomer affinity...
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[NMR paper] Solution NMR characterization of WT CXCL8 monomer and dimer binding to CXCR1 N-terminal domain.
Solution NMR characterization of WT CXCL8 monomer and dimer binding to CXCR1 N-terminal domain.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Solution NMR characterization of WT CXCL8 monomer and dimer binding to CXCR1 N-terminal domain.
Protein Sci. 2014 Oct 18;
Authors: Joseph PR, Rajarathnam K
Abstract
Chemokine CXCL8 and its receptor CXCR1 are key mediators in combating infection and have also been...
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10-21-2014 11:31 PM
Solution NMR characterization of WT CXCL8 monomer and dimer binding to CXCR1 N-terminal domain
Solution NMR characterization of WT CXCL8 monomer and dimer binding to CXCR1 N-terminal domain
Abstract
Chemokine CXCL8 and its receptor CXCR1 are key mediators in combating infection and have also been implicated in the pathophysiology of various diseases including chronic obstructive pulmonary disease (COPD) and cancer. CXCL8 exists as monomers and dimers but monomer alone binds CXCR1 with high affinity. CXCL8 function involves binding two distinct CXCR1 sites – the N-terminal domain (Site-I) and the extracellular/transmembrane domain (Site-II). Therefore, higher monomer affinity...
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[NMR paper] Direct determination of the interleukin-6 binding epitope of the interleukin-6 recept
Direct determination of the interleukin-6 binding epitope of the interleukin-6 receptor by NMR spectroscopy.
Related Articles Direct determination of the interleukin-6 binding epitope of the interleukin-6 receptor by NMR spectroscopy.
J Biol Chem. 2004 Jan 2;279(1):571-6
Authors: Schwantner A, Dingley AJ, Ozbek S, Rose-John S, Grötzinger J
All cytokines belonging to the interleukin-6 (IL-6)-type family of cytokines utilize receptors that have a modular build of several immunoglobulin-like and fibronectin type III-like domains. Characteristic...
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[NMR paper] NMR solution structure and topological orientation of monomeric phospholamban in dode
NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles.
Related Articles NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles.
Biophys J. 2003 Oct;85(4):2589-98
Authors: Zamoon J, Mascioni A, Thomas DD, Veglia G
Phospholamban is an integral membrane protein that regulates the contractility of cardiac muscle by maintaining cardiomyocyte calcium homeostasis. Abnormalities in association of protein kinase A with PLB have recently...
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[NMR paper] Solution structure of the two N-terminal RNA-binding domains of nucleolin and NMR stu
Solution structure of the two N-terminal RNA-binding domains of nucleolin and NMR study of the interaction with its RNA target.
Related Articles Solution structure of the two N-terminal RNA-binding domains of nucleolin and NMR study of the interaction with its RNA target.
J Mol Biol. 2000 Oct 20;303(2):227-41
Authors: Allain FH, Gilbert DE, Bouvet P, Feigon J
Nucleolin is an abundant 70 kDa nucleolar protein involved in many aspects of ribosomal RNA biogenesis. The central region of nucleolin contains four tandem consensus RNA-binding domains...
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[NMR paper] Determination of the solution structure of a synthetic two-site calcium-binding homod
Determination of the solution structure of a synthetic two-site calcium-binding homodimeric protein domain by NMR spectroscopy.
Related Articles Determination of the solution structure of a synthetic two-site calcium-binding homodimeric protein domain by NMR spectroscopy.
Biochemistry. 1992 Oct 13;31(40):9572-80
Authors: Shaw GS, Hodges RS, Sykes BD
The solution structure of a 34-residue synthetic calcium-binding peptide from site III of chicken troponin-C has been determined by 1H NMR spectroscopy. In solution and in the presence of calcium...
Structure of monomeric Interleukin-8 and its interactions with the N-terminal Binding Site-I of CXCR1 by solution NMR spectroscopy
Linear Mode
