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Analysis of protein-protein interaction sites using surface patches 1 1Edited by G.Von Heijne

Jones, Susan, Thornton, Janet M.·1997·Journal of Molecular Biology

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Research works printed but not linked: 66

  1. Argos, 1988, An investigation of protein subunit and domain interfaces, Protein Eng., 2, 101, 10.1093/protein/2.2.101 · DOI · Paper page
  2. Baumann, 1995, Crystal structure of a complex between Serratia marcescens metallo-protease and an inhibitor from Erwinia chrysanthemi, J. Mol. Biol., 248, 653, 10.1006/jmbi.1995.0249 · DOI
  3. Bernstein, 1977, The protein data bank, J. Mol. Biol., 112, 535, 10.1016/S0022-2836(77)80200-3 · DOI · Paper page
  4. Birktoft, 1989, Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5 Å resolution, Biochemistry, 28, 6065, 10.1021/bi00440a051 · DOI
  5. Bode, 1987, The high resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin C, an elastase inhibitor from the leech Hirudo medicinalis, Eur. J. Biochem., 166, 673, 10.1111/j.1432-1033.1987.tb13566.x · DOI · Paper page
  6. Brayer, 1983, Refined structure of the gene 5 DNA binding protein from bacteriophage fd, J. Mol. Biol., 169, 565, 10.1016/S0022-2836(83)80065-5 · doi:10.1016/s0022-2836(83)80065-5
  7. Brick, 1988, Structure of tyrosyl-tRNA synthetase refined at 2.3 Å resolution, J. Mol. Biol., 208, 83, 10.1016/0022-2836(89)90090-9 · DOI · Paper page
  8. Brunie, 1985, The refined crystal structure of dimeric phospholipase A2 at 2.5 Å, J. Biol. Chem., 260, 9742, 10.1016/S0021-9258(17)39301-8 · doi:10.1016/s0021-9258(17)39301-8
  9. Chitarra, 1993, Three-dimensional structure of a heteroclitic anitgen-antibody cross-reaction complex, Proc. Natl Acad. Sci. USA, 90, 7711, 10.1073/pnas.90.16.7711 · DOI
  10. Chothia, 1975, Principles of protein-protein recognition, Nature, 256, 705, 10.1038/256705a0 · DOI · Paper page
  11. Clore, 1990, Three dimensional structure of interleukin 8 in solution, Biochemistry, 29, 1689, 10.1021/bi00459a004 · DOI · Paper page
  12. Cohen, 1978, Covalent structural analysis of yeast inorganic pyrophosphate, J. Biol. Chem., 253, 889, 10.1016/S0021-9258(17)38188-7 · doi:10.1016/s0021-9258(17)38188-7
  13. Eklund, 1976, Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4 Å resolution, J. Mol. Biol., 102, 27, 10.1016/0022-2836(76)90072-3 · DOI · Paper page
  14. Fauchére, 1983, Hydrophobic parameters π of amino acid side chains from partitioning of N-acetyl-amino-acid amides, Eur. J. Med. Chem., 18, 369
  15. Finzel, 1985, Structure of ferricytochrome c′ from Rhodospirillum molischianum at 1.67 Å resolution, J. Mol. Biol., 186, 627, 10.1016/0022-2836(85)90135-4 · DOI · Paper page
  16. Fischmann, 1991, Crystallographic refienement of the 3-dimensional structure of the FAB D13 lysozyme complex at 2.5 angstroms, J. Biol. Chem., 266, 12915, 10.1016/S0021-9258(18)98782-X · DOI · Paper page
  17. Frigerio, 1992, Crystal and molecular structure of the bovine α-chymotrypsin-Eglin c complex at 2.0 Å resolution, J. Mol. Biol., 225, 107, 10.1016/0022-2836(92)91029-O · doi:10.1016/0022-2836(92)91029-o
  18. Fujinaga, 1987, Crystal and molecular structures of the complex of α-chymostrypsin and its inhibitor turkey ovomucoid third domain at 1.8 Å resolution, J. Mol. Biol., 195, 397, 10.1016/0022-2836(87)90659-0 · DOI · Paper page
  19. Guillet, 1993, Recognition between a bacterial ribonuclease, barnase and its natural inhibitor, barstar, Structure, 1, 165, 10.1016/0969-2126(93)90018-C · doi:10.1016/0969-2126(93)90018-c
  20. Harel, 1995, Crystal structure of an acetylcholinesterase-fasciculin complex, Structure, 3, 1355, 10.1016/S0969-2126(01)00273-8 · DOI · Paper page
  21. Hopp, 1981, Prediction of protein antigenic determinants from amino acid sequences, Proc. Natl Acad. Sci. USA, 78, 3824, 10.1073/pnas.78.6.3824 · DOI · Paper page
  22. Huang, 1993, Refined 1.6 Å resolution crystal structure of the complex formed between porcine β-trypsin and MCTAI-A, a trypsin inhibitor of the squash family, J. Mol. Biol., 229, 1022, 10.1006/jmbi.1993.1102 · doi:10.1006/jmbi.1993.1102
  23. Hurley, 1989, Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase, Proc. Natl Acad. Sci. USA, 86, 8635, 10.1073/pnas.86.22.8635 · DOI · Paper page
  24. Hurley, 1993, Structure of the regulatory complex of Escherichia coli III GLC with glycerol kinase, Science, 259, 673, 10.1126/science.8430315 · DOI · Paper page
  25. Janin, 1990, The structure of protein-protein recognition sites, J. Biol. Chem., 265, 16027, 10.1016/S0021-9258(17)46181-3 · DOI · Paper page
  26. Janin, 1988, Surface, subunit interfaces and interior of oligomeric proteins, J. Mol. Biol., 204, 155, 10.1016/0022-2836(88)90606-7 · DOI · Paper page
  27. Jin, 1992, High Resolution functional analysis of antibody-antigen interactions, J. Mol. Biol., 226, 851, 10.1016/0022-2836(92)90636-X · DOI · Paper page
  28. Jones, 1995, Protein-protein interactions, Prog. Biophys. Mol. Biol., 63, 31, 10.1016/0079-6107(94)00008-W · DOI · Paper page
  29. Jones, 1997, Prediction of protein-protein interaction sites using patch analysis, J. Mol. Biol.
  30. Korn, 1991, Distribution and complementarity of hydropathy in multisubunit proteins, Proteins: Struct. Funct. Genet., 9, 37, 10.1002/prot.340090106 · DOI
  31. Laskowski, 1996, Protein clefts in molecular recognition and function, Protein Sci., 5, 2438
  32. Lolis, 1990, Structure of yeast triosephosphate isomerase at 1.9 Å resolution, Biochemistry, 29, 6609, 10.1021/bi00480a009 · doi:10.1021/bi00480a009
  33. Lundqvist, 1991, Crystal structure of the ternary complex of ribulose-1,5-bisphosphate Mg(II), and activator CO2 at 2.3 angstroms resolution, Biochemistry, 30, 235, 10.1021/bi00218a004 · DOI
  34. Maley, 1990, Structure, multiple site binding, and segmental accommodation in thymidylate synthase on binding dUMP and anti-folate, Biochemistry, 29, 6964, 10.1021/bi00482a004 · DOI · Paper page
  35. Marquart, 1983, The geometry of the reactive site and of the peptide groups in trypsin, trypsinogen and its complexes with inhibitors, Acta Crystallog. sect. B, 39, 480, 10.1107/S010876818300275X · DOI · Paper page
  36. Miller, 1987, Interior and surface of monomeric proteins, J. Mol. Biol., 196, 641, 10.1016/0022-2836(87)90038-6 · DOI · Paper page
  37. Mitsui, 1979, Crystal structures of streptomyces subtilisin inhibitor and its complex with subtilisin BPN′, Nature, 277, 447, 10.1038/277447a0 · DOI
  38. Montfort, 1987, Refinement of C 2221 crystal form of oxidzed uteroglobin at 1.34 Å resolution, J. Mol. Biol., 194, 725, 10.1016/0022-2836(87)90250-6 · DOI
  39. Navia, 1989, Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1, Nature, 337, 615, 10.1038/337615a0 · DOI · Paper page
  40. Padlan, 1989, Structure of an antibody-antigen complex. crystal structure of the HY/HEL10 Fab lysozyme complex, Proc. Natl Acad. Sci. USA, 86, 5938, 10.1073/pnas.86.15.5938 · DOI · Paper page
  41. Pelletier, 1992, Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c, Science, 258, 1748, 10.1126/science.1334573 · DOI · Paper page
  42. Prasad, 1993, Evaluation of mutagenesis for epitope mapping, J. Biol. Chem., 268, 10705, 10.1016/S0021-9258(18)82041-5 · DOI
  43. Rees, 1990, Cardiotoxin VII4 from Naja mossambica mossambica, J. Mol. Biol., 214, 281, 10.1016/0022-2836(90)90161-E · doi:10.1016/0022-2836(90)90161-e
  44. Rees, 1982, Refined crystal structure of the potatoe inhibitor complex of carboxypeptodase at 2.5 angstroms resolution, J. Mol. Biol., 160, 475, 10.1016/0022-2836(82)90309-6 · DOI · Paper page
  45. Remington, 1982, Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 Å resolution, J. Mol. Biol., 158, 111, 10.1016/0022-2836(82)90452-1 · DOI · Paper page
  46. Royer, 1989, The 2.4 Å crystal structure of scapharca dimeric hemoglobin, J. Biol. Chem., 264, 21052, 10.1016/S0021-9258(19)30044-4 · doi:10.1016/s0021-9258(19)30044-4
  47. Savva, 1995, Nucleotide mimicry in the crystal structure of the uracil-DNA glycosylase-uracil-glycosylase inhibitor protein complex, Nature Struct. Biol., 2, 752, 10.1038/nsb0995-752 · doi:10.1038/nsb0995-752
  48. Schevitz, 1985, The 3-dimensional structure of TRP repressor, Nature, 317, 782, 10.1038/317782a0 · DOI · Paper page
  49. Schreuder, 1988, Crystal structure of p-hydroxybenzoate hydroxylase complexed with its reaction product 3,4-dihydroxybenzoate, J. Mol. Biol., 199, 638, 10.1016/0022-2836(88)90307-5 · DOI
  50. Schulz, 1982, FAD-binding site of glutathiione reductase, J. Mol. Biol., 160, 287, 10.1016/0022-2836(82)90177-2 · DOI
  51. Schutt, 1993, The structure of crystalline profilin-β-actin, Nature, 365, 810, 10.1038/365810a0 · DOI · Paper page
  52. Sheriff, 1987, Three-dimensional structure of an antibody-antigen complex, Proc. Natl Acad. Sci. USA, 84, 8075, 10.1073/pnas.84.22.8075 · DOI · Paper page
  53. Smith, 1989, 2.8 Å resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli, Biochemistry, 28, 8161, 10.1021/bi00446a030 · DOI
  54. Stec, 1990, Refined structure of yeast apo-enolase at 2.25 Å resolution, J. Mol. Biol., 211, 235, 10.1016/0022-2836(90)90023-F · DOI
  55. Stoddard, 1990, The 2.1 Å resolution structure of iron superoxide dismutase from Pseudomonas ovalis, Biochemistry, 29, 8885, 10.1021/bi00490a002 · DOI
  56. Stubbs, 1990, The refined 2.4 Å X-ray structure of recombinant human stefin B in complex with the cysteine proteinase papain, EMBO J., 6, 1939, 10.1002/j.1460-2075.1990.tb08321.x · DOI · Paper page
  57. Tainer, 1982, Determination and analysis of the 2 Å structure of copper, zinc superoxide dismutase, J. Mol. Biol., 160, 181, 10.1016/0022-2836(82)90174-7 · DOI · Paper page
  58. Takeuchi, 1991, Refined structure of the complex of subtilisin BPN′ and Streptomyces subtilisin inhibitor at 1.8 Å resolution, J. Mol. Biol., 221, 309
  59. Taylor, 1989, Protein structure alignment, J. Mol. Biol., 208, 1, 10.1016/0022-2836(89)90084-3 · DOI · Paper page
  60. Thornton, 1986, Location of “continous” antigenic determinants in the protruding regions of proteins, EMBO J., 5, 409, 10.1002/j.1460-2075.1986.tb04226.x · DOI · Paper page
  61. Tsunogae, 1986, Structure of trypsin binding domain of bowman Birk type protease inhibitor and its interaction with trypsin, J. Biochem. (Tokyo), 100, 1637, 10.1093/oxfordjournals.jbchem.a121872 · DOI
  62. Tulip, 1992, Refined crystal structure of the influenza virus N9 neuraminidase-NC41 Fab complex, J. Mol. Biol., 227, 122, 10.1016/0022-2836(92)90687-F · DOI · Paper page
  63. Weber, 1987, Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5 Å resolution, J. Mol. Biol., 198, 311, 10.1016/0022-2836(87)90315-9 · DOI · Paper page
  64. Weis, 1991, Structure of the calcium-dependent lectin domain from a rat mannose-binding protein determined by MAD phasing, Science, 254, 1608, 10.1126/science.1721241 · DOI · Paper page
  65. Winkler, 1991, Crystallization of complexes of Eco/Rv endonuclease with cognate and non-cognate /DNA fragments, J. Mol. Biol., 217, 235, 10.1016/0022-2836(91)90536-F · doi:10.1016/0022-2836(91)90536-f
  66. Young, 1994, A role for surface hydrophobicity in protein-protein recognition, Protein Sci., 3, 717, 10.1002/pro.5560030501 · DOI · Paper page

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Metadata

Authors
Jones, S., & Thornton, J. M.
Venue
Journal of Molecular Biology
Publisher
Elsevier BV
Published
1997-09
Volume
272
Issue
1
Pages
121-132
ISSN
0022-2836 (ISSN-L)
OpenAlex
W2094148990
Cited by
602
References
2
Type
book review
Language
en
Open access
closed
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

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Jones, S., & Thornton, J. M. (1997). Analysis of protein-protein interaction sites using surface patches 1 1Edited by G.Von Heijne. Journal of Molecular Biology. https://doi.org/10.1006/jmbi.1997.1234

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