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Three-dimensional structure of porcine C5adesArg from 1H nuclear magnetic resonance data.

Williamson MP, Madison VS
Biochemistry 29 2895-905 (1990)
Cited: 30 times
EuropePMC logo PMID: 2337573

Abstract

Two-dimensional nuclear magnetic resonance spectra of porcine C5adesArg (73 residues) have been used to construct a list of 34 hydrogen bonds, 27 dihedral angle constraints, and 151 distance constraints, derived from nuclear Overhauser effect data. These constraints were used in restrained molecular dynamics calculations on residues 1-65 of C5a, starting from a folded structure modeled on the crystal structure of a homologous protein, C3a. Forty-one structures have been calculated, which fall into three similar families with few violations of the imposed constraints. Structures in the most populated family have a root-mean-square deviation from the average structure of 1.02 A for the C alpha atoms, with good definition of the internal residues. There is good agreement between the calculated structures and other nuclear magnetic resonance data. The structure is very similar to that recently reported for human C5a [Zuiderweg et al. (1989) Biochemistry 28, 172-185]. Some biological implications of these structures are discussed.

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  1. Nativelike topology assembly of small proteins using predicted restraints in Monte Carlo folding simulations. Ortiz AR, Kolinski A, Skolnick J. Proc Natl Acad Sci U S A 95 1020-1025 (1998)
  2. Packing helices in proteins by global optimization of a potential energy function. Nanias M, Chinchio M, Pillardy J, Ripoll DR, Scheraga HA. Proc Natl Acad Sci U S A 100 1706-1710 (2003)
  3. Fold prediction of helical proteins using torsion angle dynamics and predicted restraints. Zhang C, Hou J, Kim SH. Proc Natl Acad Sci U S A 99 3581-3585 (2002)
  4. Iterative assembly of helical proteins by optimal hydrophobic packing. Wu GA, Coutsias EA, Dill KA. Structure 16 1257-1266 (2008)


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  1. Structure and distribution of modules in extracellular proteins. Bork P, Downing AK, Kieffer B, Campbell ID. Q Rev Biophys 29 119-167 (1996)
  2. An evaluation of computational strategies for use in the determination of protein structure from distance constraints obtained by nuclear magnetic resonance. Havel TF. Prog Biophys Mol Biol 56 43-78 (1991)
  3. Chemoattractants, extracellular proteases, and the integrated host defense response. Zabel BA, Zuniga L, Ohyama T, Allen SJ, Cichy J, Handel TM, Butcher EC. Exp Hematol 34 1021-1032 (2006)
  4. The Structural Basis of Peptide Binding at Class A G Protein-Coupled Receptors. Vu O, Bender BJ, Pankewitz L, Huster D, Beck-Sickinger AG, Meiler J. Molecules 27 210 (2021)
  5. Biomolecular structure and dynamics--experiment and theory. Forsén S, Kördel J. J Pharm Biomed Anal 14 233-236 (1996)

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  1. The C-terminal nonapeptide of mature chemerin activates the chemerin receptor with low nanomolar potency. Wittamer V, Grégoire F, Robberecht P, Vassart G, Communi D, Parmentier M. J Biol Chem 279 9956-9962 (2004)
  2. Floating stereospecific assignment revisited: application to an 18 kDa protein and comparison with J-coupling data. Folmer RH, Hilbers CW, Konings RN, Nilges M. J Biomol NMR 9 245-258 (1997)
  3. Quality assessment of NMR structures: a statistical survey. Doreleijers JF, Rullmann JA, Kaptein R. J Mol Biol 281 149-164 (1998)
  4. The structure of bovine complement component 3 reveals the basis for thioester function. Fredslund F, Jenner L, Husted LB, Nyborg J, Andersen GR, Sottrup-Jensen L. J Mol Biol 361 115-127 (2006)
  5. Structure of the streptococcal cell wall C5a peptidase. Brown CK, Gu ZY, Matsuka YV, Purushothaman SS, Winter LA, Cleary PP, Olmsted SB, Ohlendorf DH, Earhart CA. Proc Natl Acad Sci U S A 102 18391-18396 (2005)
  6. Conformational analysis of protein structures derived from NMR data. MacArthur MW, Thornton JM. Proteins 17 232-251 (1993)
  7. Structural definition of the C5a C terminus by two-dimensional nuclear magnetic resonance spectroscopy. Zhang X, Boyar W, Toth MJ, Wennogle L, Gonnella NC. Proteins 28 261-267 (1997)
  8. The topomer-sampling model of protein folding. Debe DA, Carlson MJ, Goddard WA. Proc Natl Acad Sci U S A 96 2596-2601 (1999)
  9. Residues 21-30 within the extracellular N-terminal region of the C5a receptor represent a binding domain for the C5a anaphylatoxin. Chen Z, Zhang X, Gonnella NC, Pellas TC, Boyar WC, Ni F. J Biol Chem 273 10411-10419 (1998)
  10. Cloning and functional expression of the canine anaphylatoxin C5a receptor. Evidence for high interspecies variability. Perret JJ, Raspe E, Vassart G, Parmentier M. Biochem J 288 ( Pt 3) 911-917 (1992)
  11. Two C-terminal peptides of human CKLF1 interact with the chemokine receptor CCR4. Wang Y, Zhang Y, Han W, Li D, Tian L, Yin C, Ma D. Int J Biochem Cell Biol 40 909-919 (2008)
  12. Site-specific mutagenesis of residues in the human C5a anaphylatoxin which are involved in possible interaction with the C5a receptor. Bubeck P, Grötzinger J, Winkler M, Köhl J, Wollmer A, Klos A, Bautsch W. Eur J Biochem 219 897-904 (1994)
  13. Representing an ensemble of NMR-derived protein structures by a single structure. Sutcliffe MJ. Protein Sci 2 936-944 (1993)
  14. Determination of the three-dimensional solution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coli using multidimensional NMR spectroscopy. van Nuland NA, Grötzinger J, Dijkstra K, Scheek RM, Robillard GT. Eur J Biochem 210 881-891 (1992)
  15. Primary structure and functional characterization of rat C5a: an anaphylatoxin with unusually high potency. Cui L, Carney DF, Hugli TE. Protein Sci 3 1169-1177 (1994)
  16. Structure and characterization of a high affinity C5a monoclonal antibody that blocks binding to C5aR1 and C5aR2 receptors. Colley CS, Popovic B, Sridharan S, Debreczeni JE, Hargeaves D, Fung M, An LL, Edwards B, Arnold J, England E, Eghobamien L, Sivars U, Flavell L, Renshaw J, Wickson K, Warrener P, Zha J, Bonnell J, Woods R, Wilkinson T, Dobson C, Vaughan TJ. MAbs 10 104-117 (2018)
  17. Structure of human desArg-C5a. Cook WJ, Galakatos N, Boyar WC, Walter RL, Ealick SE. Acta Crystallogr D Biol Crystallogr 66 190-197 (2010)
  18. Site-specific mutations in the N-terminal region of human C5a that affect interactions of C5a with the neutrophil C5a receptor. Carney DF, Hugli TE. Protein Sci 2 1391-1399 (1993)
  19. Solution structure of a unique C5a semi-synthetic antagonist: implications in receptor binding. Zhang X, Boyar W, Galakatos N, Gonnella NC. Protein Sci 6 65-72 (1997)
  20. Tryptophan mutants of human C5a anaphylatoxin: a fluorescence anisotropy decay and energy transfer study. Federwisch M, Wollmer A, Emde M, Stühmer T, Melcher T, Klos A, Köhl J, Bautsch W. Biophys Chem 46 237-248 (1993)
  21. C5aR ligand peptide 3D QSAR study performed with an applied linear conformation. Anderson CY, Kellogg GE, Freer RJ. J Pept Res 49 476-483 (1997)


Related citations provided by authors (1)

  1. 1H Nuclear Magnetic Resonance Assignments and Secondary Structure of Porcine C5ADesarg. Williamson MP J. Mol. Biol. 206 407- (1989)

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