Related ArticlesDetermination of the three-dimensional structure of CC chemokine monocyte chemoattractant protein 3 by 1H two-dimensional NMR spectroscopy.
MCP-3 is a beta chemokine consisting of 76 amino acid residues. It has been described to be involved in the activation of all leukocytic cells, activation mediated by the presence of multiple binding sites on the target cells. Its three-dimensional structure has been studied by making use of two-dimensional 1H NMR spectroscopy. MCP-3 exhibits the same monomeric structure as the other chemokines, i.e., a three-stranded antiparallel beta sheet covered on one face by an alpha helix. Although it belongs to the same subfamily as RANTES (Chung et al., 1995; Faitbrother et al., 1994) and hMIP-1beta (Lodi et al., 1994), the MCP-3 dimer is folded like IL-8 with the so-called alphabeta sandwich structural motif. Structural and sequence analysis gives clear indications suggesting that the other MCP chemokines may have the same quaternary structure, contrary to the other beta chemokines.
[NMR paper] Determination of the three-dimensional solution structure of Raphanus sativus antifun
Determination of the three-dimensional solution structure of Raphanus sativus antifungal protein 1 by 1H NMR.
Related Articles Determination of the three-dimensional solution structure of Raphanus sativus antifungal protein 1 by 1H NMR.
J Mol Biol. 1998 May 29;279(1):257-70
Authors: Fant F, Vranken W, Broekaert W, Borremans F
Raphanus sativus Antifungal Protein 1 (Rs-AFP1) is a 51 amino acid residue plant defensin isolated from radish (Raphanus sativus L.) seeds. The three-dimensional structure in aqueous solution has been determined from...
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[NMR paper] Determination of the three-dimensional structure of CC chemokine monocyte chemoattrac
Determination of the three-dimensional structure of CC chemokine monocyte chemoattractant protein 3 by 1H two-dimensional NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Determination of the three-dimensional structure of CC chemokine monocyte chemoattractant protein 3 by 1H two-dimensional NMR spectroscopy.
Biochemistry. 1997 Apr 15;36(15):4412-22
Authors: Meunier S, Bernassau JM, Guillemot JC, Ferrara P, Darbon H
MCP-3 is a beta chemokine consisting of 76 amino acid...
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[NMR paper] Heteronuclear (1H, 13C, 15N) NMR assignments and solution structure of the monocyte c
Heteronuclear (1H, 13C, 15N) NMR assignments and solution structure of the monocyte chemoattractant protein-1 (MCP-1) dimer.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Heteronuclear (1H, 13C, 15N) NMR assignments and solution structure of the monocyte chemoattractant protein-1 (MCP-1) dimer.
Biochemistry. 1996 May 28;35(21):6569-84
Authors: Handel TM, Domaille PJ
A full high-resolution three-dimensional solution structure of the monocyte chemoattractant protein-1 (MCP-1 or MCAF)...
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[NMR paper] High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensio
High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR.
Related Articles High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR.
Science. 1994 Mar 25;263(5154):1762-7
Authors: Lodi PJ, Garrett DS, Kuszewski J, Tsang ML, Weatherbee JA, Leonard WJ, Gronenborn AM, Clore GM
The three-dimensional structure of a member of the beta subfamily of chemokines, human macrophage inflammatory protein-1 beta (hMIP-1 beta), has been determined with the use of solution multidimensional...
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[NMR paper] Primary and NMR three-dimensional structure determination of a novel crustacean toxin
Primary and NMR three-dimensional structure determination of a novel crustacean toxin from the venom of the scorpion Centruroides limpidus limpidus Karsch.
Related Articles Primary and NMR three-dimensional structure determination of a novel crustacean toxin from the venom of the scorpion Centruroides limpidus limpidus Karsch.
Biochemistry. 1994 Sep 20;33(37):11135-49
Authors: Lebreton F, Delepierre M, RamÃ*rez AN, Balderas C, Possani LD
A crustacean-specific toxin from the Mexican scorpion Centruroides limpidus limpidus was purified, and its...
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[NMR paper] NMR determination of the secondary structure and the three-dimensional polypeptide ba
NMR determination of the secondary structure and the three-dimensional polypeptide backbone fold of the human sterol carrier protein 2.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR determination of the secondary structure and the three-dimensional polypeptide backbone fold of the human sterol carrier protein 2.
FEBS Lett. 1993 Nov 29;335(1):18-26
Authors: Szyperski T, Scheek S, Johansson J, Assmann G, Seedorf U, Wüthrich K
Nuclear magnetic resonance (NMR)...
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[NMR paper] 1H NMR-based determination of the three-dimensional structure of the human plasma fib
1H NMR-based determination of the three-dimensional structure of the human plasma fibronectin fragment containing inter-chain disulfide bonds.
Related Articles 1H NMR-based determination of the three-dimensional structure of the human plasma fibronectin fragment containing inter-chain disulfide bonds.
J Biol Chem. 1993 Apr 25;268(12):8580-9
Authors: Kar L, Lai CS, Wolff CE, Nettesheim D, Sherman S, Johnson ME
Human plasma fibronectin is a plasma glycoprotein that plays an important role in many biological processes. It consists of two...
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[NMR paper] Determination of the three-dimensional solution structure of the histidine-containing
Determination of the three-dimensional solution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coli using multidimensional NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Determination of the three-dimensional solution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coli using multidimensional NMR spectroscopy.
Eur J Biochem. 1992 Dec 15;210(3):881-91
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