메뉴 건너뛰기




Volumn 398, Issue 1, 2010, Pages 146-160

The subunit interfaces of weakly associated homodimeric proteins

Author keywords

Amino acid propensity; Atomic packing density; Interface area; Monomer dimer equilibrium; Protein protein interaction

Indexed keywords

4ALPHA GLUCANOTRANSFERASE; ALPHA CRYSTALLIN; ANTIBODY; ANTIGEN; ASIALOGLYCOPROTEIN; BETA LACTOGLOBULIN; CARBOXYLESTERASE; CELLULAR RETINOL BINDING PROTEIN 1; CILIARY NEUROTROPHIC FACTOR; COPPER ZINC SUPEROXIDE DISMUTASE; COXSACKIE VIRUS AND ADENOVIRUS RECEPTOR; DIMER; FIBROBLAST GROWTH FACTOR 9; GALECTIN; HETERODIMER; HOMODIMER; INTERLEUKIN 8; MANGANESE SUPEROXIDE DISMUTASE; MONOCYTE CHEMOTACTIC PROTEIN 1; MONOMER; MYELIN OLIGODENDROCYTE GLYCOPROTEIN; PHOSPHORIBOSYLTRANSFERASE; PROTEIN; PROTEIN SUBUNIT; PROTEINASE INHIBITOR; STEM CELL FACTOR; THIOREDOXIN; UVOMORULIN; VIRUS PROTEIN; WATER;

EID: 77950867698     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.02.020     Document Type: Article
Times cited : (95)

References (111)
  • 2
    • 0023193446 scopus 로고
    • The accessible surface area and stability of oligomeric proteins
    • Miller S., Lesk A.M., Janin J., Chothia C. The accessible surface area and stability of oligomeric proteins. Nature 1987, 328:834-836.
    • (1987) Nature , vol.328 , pp. 834-836
    • Miller, S.1    Lesk, A.M.2    Janin, J.3    Chothia, C.4
  • 3
    • 0024246956 scopus 로고
    • Surface, subunit interfaces and interior of oligomeric proteins
    • Janin J., Miller S., Chothia C. Surface, subunit interfaces and interior of oligomeric proteins. J. Mol. Biol. 1988, 204:155-164.
    • (1988) J. Mol. Biol. , vol.204 , pp. 155-164
    • Janin, J.1    Miller, S.2    Chothia, C.3
  • 4
    • 0024046505 scopus 로고
    • An investigation of protein subunit and domain interfaces
    • Argos P. An investigation of protein subunit and domain interfaces. Protein Eng. 1988, 2:101-113.
    • (1988) Protein Eng. , vol.2 , pp. 101-113
    • Argos, P.1
  • 5
    • 0025123333 scopus 로고
    • The structure of protein-protein recognition sites
    • Janin J., Chothia C. The structure of protein-protein recognition sites. J. Biol. Chem. 1990, 265:16027-16030.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16027-16030
    • Janin, J.1    Chothia, C.2
  • 6
    • 0029109468 scopus 로고
    • Protein-protein interactions: a review of protein dimer structures
    • Jones S., Thornton J.M. Protein-protein interactions: a review of protein dimer structures. Prog. Biophys. Mol. Biol. 1995, 63:31-65.
    • (1995) Prog. Biophys. Mol. Biol. , vol.63 , pp. 31-65
    • Jones, S.1    Thornton, J.M.2
  • 7
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones S., Thornton J.M. Principles of protein-protein interactions. Proc. Natl Acad. Sci. USA 1996, 1996:13-20.
    • (1996) Proc. Natl Acad. Sci. USA , vol.1996 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 8
    • 0030602896 scopus 로고    scopus 로고
    • A dataset of protein-protein interfaces generated with a sequence-order-independent comparison technique
    • Tsai C.J., Lin S.L., Wolfson H.J., Nussinov R. A dataset of protein-protein interfaces generated with a sequence-order-independent comparison technique. J. Mol. Biol. 1996, 260:604-620.
    • (1996) J. Mol. Biol. , vol.260 , pp. 604-620
    • Tsai, C.J.1    Lin, S.L.2    Wolfson, H.J.3    Nussinov, R.4
  • 9
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Lo Conte L., Chothia C., Janin J. The atomic structure of protein-protein recognition sites. J. Mol. Biol. 1999, 285:2177-2198.
    • (1999) J. Mol. Biol. , vol.285 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 10
    • 0034308172 scopus 로고    scopus 로고
    • Discriminating between homodimeric and monomeric proteins in the crystalline state
    • Ponstingl H., Henrick K., Thornton J.M. Discriminating between homodimeric and monomeric proteins in the crystalline state. Proteins 2000, 41:47-57.
    • (2000) Proteins , vol.41 , pp. 47-57
    • Ponstingl, H.1    Henrick, K.2    Thornton, J.M.3
  • 11
    • 0037093645 scopus 로고    scopus 로고
    • Dissecting protein-protein recognition sites
    • Chakrabarti P., Janin J. Dissecting protein-protein recognition sites. Proteins 2002, 47:334-343.
    • (2002) Proteins , vol.47 , pp. 334-343
    • Chakrabarti, P.1    Janin, J.2
  • 12
    • 0041312697 scopus 로고    scopus 로고
    • Diversity of protein-protein interactions
    • Nooren I.M.A., Thornton J.M. Diversity of protein-protein interactions. EMBO J. 2003, 22:3486-3492.
    • (2003) EMBO J. , vol.22 , pp. 3486-3492
    • Nooren, I.M.A.1    Thornton, J.M.2
  • 13
    • 0242299201 scopus 로고    scopus 로고
    • Dissecting subunit interfaces in homodimeric proteins
    • Bahadur R.P., Chakrabarti P., Rodier F., Janin J. Dissecting subunit interfaces in homodimeric proteins. Proteins 2003, 53:708-719.
    • (2003) Proteins , vol.53 , pp. 708-719
    • Bahadur, R.P.1    Chakrabarti, P.2    Rodier, F.3    Janin, J.4
  • 14
    • 1042275583 scopus 로고    scopus 로고
    • A dissection of specific and non-specific protein-protein interfaces
    • Bahadur R.P., Chakrabarti P., Rodier F., Janin J. A dissection of specific and non-specific protein-protein interfaces. J. Mol. Biol. 2004, 336:943-955.
    • (2004) J. Mol. Biol. , vol.336 , pp. 943-955
    • Bahadur, R.P.1    Chakrabarti, P.2    Rodier, F.3    Janin, J.4
  • 16
    • 52649130704 scopus 로고    scopus 로고
    • Protein-protein interaction and quaternary structure
    • Janin J., Bahadur R.P., Chakrabarti P. Protein-protein interaction and quaternary structure. Q. Rev. Biophys. 2008, 41:133-180.
    • (2008) Q. Rev. Biophys. , vol.41 , pp. 133-180
    • Janin, J.1    Bahadur, R.P.2    Chakrabarti, P.3
  • 17
    • 70349229596 scopus 로고    scopus 로고
    • Dynamic interactions of proteins in complex networks: a more structured view
    • Stein A., Pache R.A., Bernadó P., Pons M., Aloy P. Dynamic interactions of proteins in complex networks: a more structured view. FEBS J. 2009, 276:5390-5405.
    • (2009) FEBS J. , vol.276 , pp. 5390-5405
    • Stein, A.1    Pache, R.A.2    Bernadó, P.3    Pons, M.4    Aloy, P.5
  • 19
    • 0037474541 scopus 로고    scopus 로고
    • Structural characterisation and functional significance of transient protein-protein interactions
    • Nooren I.M.A., Thornton J.M. Structural characterisation and functional significance of transient protein-protein interactions. J. Mol. Biol. 2003, 325:991-1018.
    • (2003) J. Mol. Biol. , vol.325 , pp. 991-1018
    • Nooren, I.M.A.1    Thornton, J.M.2
  • 20
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E., Henrick K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 2007, 372:774-797.
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 22
    • 35748959334 scopus 로고    scopus 로고
    • PiQSi: protein quaternary structure investigation
    • Levy E.D. PiQSi: protein quaternary structure investigation. Structure 2007, 15:1364-1367.
    • (2007) Structure , vol.15 , pp. 1364-1367
    • Levy, E.D.1
  • 23
    • 0032169688 scopus 로고    scopus 로고
    • PQS: a protein quaternary structure file server
    • Henrick K., Thornton J.M. PQS: a protein quaternary structure file server. Trends Biochem. Sci. 1998, 23:358-361.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 358-361
    • Henrick, K.1    Thornton, J.M.2
  • 24
    • 0043180474 scopus 로고    scopus 로고
    • PISCES: a protein sequence culling server
    • Wang G., Dunbrack R.L. PISCES: a protein sequence culling server. Bioinformatics 2003, 19:1589-1591.
    • (2003) Bioinformatics , vol.19 , pp. 1589-1591
    • Wang, G.1    Dunbrack, R.L.2
  • 25
    • 0032499791 scopus 로고    scopus 로고
    • Crystal structure of chemically synthesized [N33A] stromal cell-derived factor 1alpha, a potent ligand for the HIV-1 "fusin" coreceptor
    • Dealwis C., Fernandez E.J., Thompson D.A., Simon R.J., Siani M.A., Lolis E. Crystal structure of chemically synthesized [N33A] stromal cell-derived factor 1alpha, a potent ligand for the HIV-1 "fusin" coreceptor. Proc. Natl Acad. Sci. USA 1998, 95:6941-6946.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6941-6946
    • Dealwis, C.1    Fernandez, E.J.2    Thompson, D.A.3    Simon, R.J.4    Siani, M.A.5    Lolis, E.6
  • 26
    • 0030710251 scopus 로고    scopus 로고
    • Towards a molecular understanding of phase separation in the lens: a comparison of the X-ray structures of two high Tc gamma-crystallins, gammaE and gammaF, with two low Tc gamma-crystallins, gammaB and gammaD
    • Norledge B.V., Hay R.E., Bateman O.A., Slingsby C., Driessen H.P. Towards a molecular understanding of phase separation in the lens: a comparison of the X-ray structures of two high Tc gamma-crystallins, gammaE and gammaF, with two low Tc gamma-crystallins, gammaB and gammaD. Exp. Eye Res. 1997, 65:609-630.
    • (1997) Exp. Eye Res. , vol.65 , pp. 609-630
    • Norledge, B.V.1    Hay, R.E.2    Bateman, O.A.3    Slingsby, C.4    Driessen, H.P.5
  • 27
    • 0034663733 scopus 로고    scopus 로고
    • Soluble beta-galactosyl-binding lectin (galectin) from toad ovary: crystallographic studies of two protein-sugar complexes
    • Bianchet M.A., Ahmed H., Vasta G.R., Amzel L.M. Soluble beta-galactosyl-binding lectin (galectin) from toad ovary: crystallographic studies of two protein-sugar complexes. Proteins 2000, 40:378-388.
    • (2000) Proteins , vol.40 , pp. 378-388
    • Bianchet, M.A.1    Ahmed, H.2    Vasta, G.R.3    Amzel, L.M.4
  • 28
    • 0029800459 scopus 로고    scopus 로고
    • Characterization of monomeric forms of galectin-1 generated by site-directed mutagenesis
    • Cho M., Cummings R.D. Characterization of monomeric forms of galectin-1 generated by site-directed mutagenesis. Biochemistry 1996, 35:13081-13088.
    • (1996) Biochemistry , vol.35 , pp. 13081-13088
    • Cho, M.1    Cummings, R.D.2
  • 29
    • 0034825616 scopus 로고    scopus 로고
    • Crystal structures of bovine beta-lactoglobulin in the orthorhombic space group C222(1). Structural differences between genetic variants A and B and features of the Tanford transition
    • Oliveira K.M., Valente-Mesquita V.L., Botelho M.M., Sawyer L., Ferreira S.T., Polikarpov I. Crystal structures of bovine beta-lactoglobulin in the orthorhombic space group C222(1). Structural differences between genetic variants A and B and features of the Tanford transition. Eur. J. Biochem. 2001, 268:477-483.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 477-483
    • Oliveira, K.M.1    Valente-Mesquita, V.L.2    Botelho, M.M.3    Sawyer, L.4    Ferreira, S.T.5    Polikarpov, I.6
  • 30
    • 0034769732 scopus 로고    scopus 로고
    • Salt-dependent monomer-dimer equilibrium of bovine beta-lactoglobulin at pH 3
    • Sakurai K., Oobatake M., Goto Y. Salt-dependent monomer-dimer equilibrium of bovine beta-lactoglobulin at pH 3. Protein Sci. 2001, 10:2325-2335.
    • (2001) Protein Sci. , vol.10 , pp. 2325-2335
    • Sakurai, K.1    Oobatake, M.2    Goto, Y.3
  • 31
    • 0027380310 scopus 로고
    • Atomic structure of a cytochrome c' with an unusual ligand-controlled dimer dissociation at 1.8 Å resolution
    • Ren Z., Meyer T., McRee D.E. Atomic structure of a cytochrome c' with an unusual ligand-controlled dimer dissociation at 1.8 Å resolution. J. Mol. Biol. 1993, 234:433-445.
    • (1993) J. Mol. Biol. , vol.234 , pp. 433-445
    • Ren, Z.1    Meyer, T.2    McRee, D.E.3
  • 32
    • 0031573470 scopus 로고    scopus 로고
    • The role of DNA in the mechanism of NFkappaB dimer formation: crystal structures of the dimerization domains of the p50 and p65 subunits
    • Huang D.B., Huxford T., Chen Y.Q., Ghosh G. The role of DNA in the mechanism of NFkappaB dimer formation: crystal structures of the dimerization domains of the p50 and p65 subunits. Structure 1997, 5:1427-1436.
    • (1997) Structure , vol.5 , pp. 1427-1436
    • Huang, D.B.1    Huxford, T.2    Chen, Y.Q.3    Ghosh, G.4
  • 33
    • 0029125852 scopus 로고
    • Crystal structure of cellular retinoic acid binding protein I shows increased access to the binding cavity due to formation of an intermolecular beta-sheet
    • Thompson J.R., Bratt J.M., Banaszak L.J. Crystal structure of cellular retinoic acid binding protein I shows increased access to the binding cavity due to formation of an intermolecular beta-sheet. J. Mol. Biol. 1995, 252:433-446.
    • (1995) J. Mol. Biol. , vol.252 , pp. 433-446
    • Thompson, J.R.1    Bratt, J.M.2    Banaszak, L.J.3
  • 34
    • 0034622583 scopus 로고    scopus 로고
    • Dynamics of cellular retinoic acid binding protein I on multiple time scales with implications for ligand binding
    • Krishnan V.V., Sukumar M., Gierasch L.M., Cosman M. Dynamics of cellular retinoic acid binding protein I on multiple time scales with implications for ligand binding. Biochemistry 2000, 39:9119-9129.
    • (2000) Biochemistry , vol.39 , pp. 9119-9129
    • Krishnan, V.V.1    Sukumar, M.2    Gierasch, L.M.3    Cosman, M.4
  • 35
    • 0029046795 scopus 로고
    • Crystal structure of dimeric human ciliary neurotrophic factor determined by MAD phasing
    • McDonald N.Q., Panayotatos N., Hendrickson W.A. Crystal structure of dimeric human ciliary neurotrophic factor determined by MAD phasing. EMBO J. 1995, 14:2689-2699.
    • (1995) EMBO J. , vol.14 , pp. 2689-2699
    • McDonald, N.Q.1    Panayotatos, N.2    Hendrickson, W.A.3
  • 36
    • 0033550058 scopus 로고    scopus 로고
    • Atomic resolution structures of the core domain of avian sarcoma virus integrase and its D64N mutant
    • Lubkowski J., Dauter Z., Yang F., Alexandratos J., Merkel G., Skalka A.M., Wlodawer A. Atomic resolution structures of the core domain of avian sarcoma virus integrase and its D64N mutant. Biochemistry 1999, 38:13512-13522.
    • (1999) Biochemistry , vol.38 , pp. 13512-13522
    • Lubkowski, J.1    Dauter, Z.2    Yang, F.3    Alexandratos, J.4    Merkel, G.5    Skalka, A.M.6    Wlodawer, A.7
  • 37
    • 0032755249 scopus 로고    scopus 로고
    • Characterization of the self association of avian sarcoma virus integrase by analytical ultracentrifugation
    • Coleman J., Eaton S., Merkel G., Skalka A.M., Laue T. Characterization of the self association of avian sarcoma virus integrase by analytical ultracentrifugation. J. Biol. Chem. 1999, 274:32842-32846.
    • (1999) J. Biol. Chem. , vol.274 , pp. 32842-32846
    • Coleman, J.1    Eaton, S.2    Merkel, G.3    Skalka, A.M.4    Laue, T.5
  • 38
    • 0030597050 scopus 로고    scopus 로고
    • Structural characterization of a monomeric chemokine: monocyte chemoattractant protein-3
    • Kim K.S., Rajarathnam K., Clark-Lewis I., Sykes B.D. Structural characterization of a monomeric chemokine: monocyte chemoattractant protein-3. FEBS Lett. 1996, 395:277-282.
    • (1996) FEBS Lett. , vol.395 , pp. 277-282
    • Kim, K.S.1    Rajarathnam, K.2    Clark-Lewis, I.3    Sykes, B.D.4
  • 39
    • 0034677527 scopus 로고    scopus 로고
    • Structure of the intact transactivation domain of the human papillomavirus E2 protein
    • Antson A.A., Burns J.E., Moroz O.V., Scott D.J., Sanders C.M., Bronstein I.B., et al. Structure of the intact transactivation domain of the human papillomavirus E2 protein. Nature 2000, 403:805-809.
    • (2000) Nature , vol.403 , pp. 805-809
    • Antson, A.A.1    Burns, J.E.2    Moroz, O.V.3    Scott, D.J.4    Sanders, C.M.5    Bronstein, I.B.6
  • 40
    • 0034697981 scopus 로고    scopus 로고
    • Crystal structure of the carbohydrate recognition domain of the H1 subunit of the asialoglycoprotein receptor
    • Meier M., Bider M.D., Malashkevich V.N., Spiess M., Burkhard P. Crystal structure of the carbohydrate recognition domain of the H1 subunit of the asialoglycoprotein receptor. J. Mol. Biol. 2000, 300:857-865.
    • (2000) J. Mol. Biol. , vol.300 , pp. 857-865
    • Meier, M.1    Bider, M.D.2    Malashkevich, V.N.3    Spiess, M.4    Burkhard, P.5
  • 41
    • 0035831550 scopus 로고    scopus 로고
    • Crystal structure of the C-type lectin-like domain from the human hematopoietic cell receptor CD69
    • Llera A.S., Viedma F., Sánchez-Madrid F., Tormo J. Crystal structure of the C-type lectin-like domain from the human hematopoietic cell receptor CD69. J. Biol. Chem. 2001, 276:7312-7319.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7312-7319
    • Llera, A.S.1    Viedma, F.2    Sánchez-Madrid, F.3    Tormo, J.4
  • 42
    • 0034435587 scopus 로고    scopus 로고
    • Dimeric structure of the coxsackievirus and adenovirus receptor D1 domain at 1.7 Å resolution
    • van Raaij M.J., Chouin E., van der Zandt H., Bergelson J.M., Cusack S. Dimeric structure of the coxsackievirus and adenovirus receptor D1 domain at 1.7 Å resolution. Structure 2000, 8:1147-1155.
    • (2000) Structure , vol.8 , pp. 1147-1155
    • van Raaij, M.J.1    Chouin, E.2    van der Zandt, H.3    Bergelson, J.M.4    Cusack, S.5
  • 43
    • 0029980542 scopus 로고    scopus 로고
    • Structural basis of calcium-induced E-cadherin rigidification and dimerization
    • Nagar B., Overduin M., Ikura M., Rini J.M. Structural basis of calcium-induced E-cadherin rigidification and dimerization. Nature 1996, 380:360-364.
    • (1996) Nature , vol.380 , pp. 360-364
    • Nagar, B.1    Overduin, M.2    Ikura, M.3    Rini, J.M.4
  • 44
    • 0036217934 scopus 로고    scopus 로고
    • Increasing protein stability by polar surface residues: domain-wide consequences of interactions within a loop
    • Pokkuluri P.R., Raffen R., Dieckman L., Boogaard C., Stevens F.J., Schiffer M. Increasing protein stability by polar surface residues: domain-wide consequences of interactions within a loop. Biophys. J. 2002, 82:391-398.
    • (2002) Biophys. J. , vol.82 , pp. 391-398
    • Pokkuluri, P.R.1    Raffen, R.2    Dieckman, L.3    Boogaard, C.4    Stevens, F.J.5    Schiffer, M.6
  • 45
    • 0030585429 scopus 로고    scopus 로고
    • Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer
    • Weichsel A., Gasdaska J.R., Powis G., Montfort W.R. Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer. Structure 1996, 4:735-751.
    • (1996) Structure , vol.4 , pp. 735-751
    • Weichsel, A.1    Gasdaska, J.R.2    Powis, G.3    Montfort, W.R.4
  • 46
    • 0030671351 scopus 로고    scopus 로고
    • Human thioredoxin homodimers: regulation by pH, role of aspartate 60, and crystal structure of the aspartate 60→asparagine mutant
    • Andersen J.F., Sanders D.A., Gasdaska J.R., Weichsel A., Powis G., Montfort W.R. Human thioredoxin homodimers: regulation by pH, role of aspartate 60, and crystal structure of the aspartate 60→asparagine mutant. Biochemistry 1997, 36:13979-13988.
    • (1997) Biochemistry , vol.36 , pp. 13979-13988
    • Andersen, J.F.1    Sanders, D.A.2    Gasdaska, J.R.3    Weichsel, A.4    Powis, G.5    Montfort, W.R.6
  • 47
    • 0034608859 scopus 로고    scopus 로고
    • Crystal structure of human stem cell factor: implication for stem cell factor receptor dimerization and activation
    • Zhang Z., Zhang R., Joachimiak A., Schlessinger J., Kong X.P. Crystal structure of human stem cell factor: implication for stem cell factor receptor dimerization and activation. Proc. Natl Acad. Sci. USA 2000, 97:7732-7737.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 7732-7737
    • Zhang, Z.1    Zhang, R.2    Joachimiak, A.3    Schlessinger, J.4    Kong, X.P.5
  • 48
    • 0028797816 scopus 로고
    • Spontaneous dissociation-association of monomers of the human-stem-cell-factor dimer
    • Lu H.S., Chang W.C., Mendiaz E.A., Mann M.B., Langley K.E., Hsu Y.R. Spontaneous dissociation-association of monomers of the human-stem-cell-factor dimer. Biochem. J. 1995, 305:563-568.
    • (1995) Biochem. J. , vol.305 , pp. 563-568
    • Lu, H.S.1    Chang, W.C.2    Mendiaz, E.A.3    Mann, M.B.4    Langley, K.E.5    Hsu, Y.R.6
  • 49
    • 0035983515 scopus 로고    scopus 로고
    • Crystal structure of the CCTgamma apical domain: implications for substrate binding to the eukaryotic cytosolic chaperonin
    • Pappenberger G., Wilsher J.A., Roe S.M., Counsell D.J., Willison K.R., Pearl L.H. Crystal structure of the CCTgamma apical domain: implications for substrate binding to the eukaryotic cytosolic chaperonin. J. Mol. Biol. 2002, 318:1367-1379.
    • (2002) J. Mol. Biol. , vol.318 , pp. 1367-1379
    • Pappenberger, G.1    Wilsher, J.A.2    Roe, S.M.3    Counsell, D.J.4    Willison, K.R.5    Pearl, L.H.6
  • 50
    • 0036171554 scopus 로고    scopus 로고
    • Crystal structure of pea Toc34, a novel GTPase of the chloroplast protein translocon
    • Sun Y.J., Forouhar F., Li H.M., Tu S.L., Yeh Y.H., Kao S., et al. Crystal structure of pea Toc34, a novel GTPase of the chloroplast protein translocon. Nat. Struct. Biol. 2002, 9:95-100.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 95-100
    • Sun, Y.J.1    Forouhar, F.2    Li, H.M.3    Tu, S.L.4    Yeh, Y.H.5    Kao, S.6
  • 51
    • 0029898439 scopus 로고    scopus 로고
    • Crystal structure of the hypoxanthine-guanine-xanthine phosphoribosyltransferase from the protozoan parasite Tritrichomonas foetus
    • Somoza J.R., Chin M.S., Focia P.J., Wang C.C., Fletterick R.J. Crystal structure of the hypoxanthine-guanine-xanthine phosphoribosyltransferase from the protozoan parasite Tritrichomonas foetus. Biochemistry 1996, 35:7032-7040.
    • (1996) Biochemistry , vol.35 , pp. 7032-7040
    • Somoza, J.R.1    Chin, M.S.2    Focia, P.J.3    Wang, C.C.4    Fletterick, R.J.5
  • 53
    • 0035943408 scopus 로고    scopus 로고
    • Mechanisms for ligand binding to GluR0 ion channels: crystal structures of the glutamate and serine complexes and a closed apo state
    • Mayer M.L., Olson R., Gouaux E. Mechanisms for ligand binding to GluR0 ion channels: crystal structures of the glutamate and serine complexes and a closed apo state. J. Mol. Biol. 2001, 311:815-836.
    • (2001) J. Mol. Biol. , vol.311 , pp. 815-836
    • Mayer, M.L.1    Olson, R.2    Gouaux, E.3
  • 55
    • 6444245095 scopus 로고    scopus 로고
    • Three-dimensional structure of manganese superoxide dismutase from Bacillus halodenitrificans, a component of the so-called "green protein"
    • Liao J., Liu M.Y., Chang T., Li M., Le Gall J., Gui L.L., et al. Three-dimensional structure of manganese superoxide dismutase from Bacillus halodenitrificans, a component of the so-called "green protein". J. Struct. Biol. 2002, 139:171-180.
    • (2002) J. Struct. Biol. , vol.139 , pp. 171-180
    • Liao, J.1    Liu, M.Y.2    Chang, T.3    Li, M.4    Le Gall, J.5    Gui, L.L.6
  • 56
    • 0036354161 scopus 로고    scopus 로고
    • Crystal structure of Thermotoga maritima 4-alpha-glucanotransferase and its acarbose complex: implications for substrate specificity and catalysis
    • Roujeinikova A., Raasch C., Sedelnikova S., Liebl W., Rice D.W. Crystal structure of Thermotoga maritima 4-alpha-glucanotransferase and its acarbose complex: implications for substrate specificity and catalysis. J. Mol. Biol. 2002, 321:149-162.
    • (2002) J. Mol. Biol. , vol.321 , pp. 149-162
    • Roujeinikova, A.1    Raasch, C.2    Sedelnikova, S.3    Liebl, W.4    Rice, D.W.5
  • 57
    • 0030246987 scopus 로고    scopus 로고
    • Crystal structure of the extracellular domain from P0, the major structural protein of peripheral nerve myelin
    • Shapiro L., Doyle J.P., Hensley P., Colman D.R., Hendrickson W.A. Crystal structure of the extracellular domain from P0, the major structural protein of peripheral nerve myelin. Neuron 1996, 17:435-449.
    • (1996) Neuron , vol.17 , pp. 435-449
    • Shapiro, L.1    Doyle, J.P.2    Hensley, P.3    Colman, D.R.4    Hendrickson, W.A.5
  • 58
    • 0037969630 scopus 로고    scopus 로고
    • Structural basis for dimerization of the Grb10 Src homology 2 domain. Implications for ligand specificity
    • Stein E.G., Ghirlando R., Hubbard S.R. Structural basis for dimerization of the Grb10 Src homology 2 domain. Implications for ligand specificity. J. Biol. Chem. 2003, 278:13257-13264.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13257-13264
    • Stein, E.G.1    Ghirlando, R.2    Hubbard, S.R.3
  • 60
    • 0037424626 scopus 로고    scopus 로고
    • Active-site copper and zinc ions modulate the quaternary structure of prokaryotic Cu,Zn superoxide dismutase
    • Cioni P., Pesce A., Morozzo della Rocca B., Castelli S., Falconi M., Parrilli L., et al. Active-site copper and zinc ions modulate the quaternary structure of prokaryotic Cu,Zn superoxide dismutase. J. Mol. Biol. 2003, 326:1351-1360.
    • (2003) J. Mol. Biol. , vol.326 , pp. 1351-1360
    • Cioni, P.1    Pesce, A.2    Morozzo della Rocca, B.3    Castelli, S.4    Falconi, M.5    Parrilli, L.6
  • 62
    • 0141703197 scopus 로고    scopus 로고
    • The crystal structure of myelin oligodendrocyte glycoprotein, a key autoantigen in multiple sclerosis
    • Clements C.S., Reid H.H., Beddoe T., Tynan F.E., Perugini M.A., Johns T.G., et al. The crystal structure of myelin oligodendrocyte glycoprotein, a key autoantigen in multiple sclerosis. Proc. Natl Acad. Sci. USA 2003, 100:11059-11064.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 11059-11064
    • Clements, C.S.1    Reid, H.H.2    Beddoe, T.3    Tynan, F.E.4    Perugini, M.A.5    Johns, T.G.6
  • 64
    • 0029868999 scopus 로고    scopus 로고
    • Crystal structure of the rat liver fructose-2,6-bisphosphatase based on selenomethionine multiwavelength anomalous dispersion phases
    • Lee Y.H., Ogata C., Pflugrath J.W., Levitt D.G., Sarma R., Banaszak L.J., Pilkis S.J. Crystal structure of the rat liver fructose-2,6-bisphosphatase based on selenomethionine multiwavelength anomalous dispersion phases. Biochemistry 1996, 35:6010-6019.
    • (1996) Biochemistry , vol.35 , pp. 6010-6019
    • Lee, Y.H.1    Ogata, C.2    Pflugrath, J.W.3    Levitt, D.G.4    Sarma, R.5    Banaszak, L.J.6    Pilkis, S.J.7
  • 65
    • 1642539986 scopus 로고    scopus 로고
    • The effect of mutations surrounding and within the active site on the catalytic activity of ricin A chain
    • Marsden C.J., Fülöp V., Day P.J., Lord J.M. The effect of mutations surrounding and within the active site on the catalytic activity of ricin A chain. Eur. J. Biochem. 2004, 271:153-162.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 153-162
    • Marsden, C.J.1    Fülöp, V.2    Day, P.J.3    Lord, J.M.4
  • 66
    • 0030586822 scopus 로고    scopus 로고
    • The role of the divalent cation in the structure of the I domain from the CD11a/CD18 integrin
    • Qu A., Leahy D.J. The role of the divalent cation in the structure of the I domain from the CD11a/CD18 integrin. Structure 1996, 4:931-942.
    • (1996) Structure , vol.4 , pp. 931-942
    • Qu, A.1    Leahy, D.J.2
  • 67
    • 0029739483 scopus 로고    scopus 로고
    • High-resolution structure of the diphtheria toxin repressor complexed with cobalt and manganese reveals an SH3-like third domain and suggests a possible role of phosphate as co-corepressor
    • Qiu X., Pohl E., Holmes R.K., Hol W.G. High-resolution structure of the diphtheria toxin repressor complexed with cobalt and manganese reveals an SH3-like third domain and suggests a possible role of phosphate as co-corepressor. Biochemistry 1996, 35:12292-12302.
    • (1996) Biochemistry , vol.35 , pp. 12292-12302
    • Qiu, X.1    Pohl, E.2    Holmes, R.K.3    Hol, W.G.4
  • 68
    • 0033980359 scopus 로고    scopus 로고
    • 1.35 and 2.07 Å resolution structures of the red abalone sperm lysin monomer and dimer reveal features involved in receptor binding
    • Kresge N., Vacquier V.D., Stout C.D. 1.35 and 2.07 Å resolution structures of the red abalone sperm lysin monomer and dimer reveal features involved in receptor binding. Acta Crystallogr., Sect. D: Biol. Crystallogr. 2000, 56:34-41.
    • (2000) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.56 , pp. 34-41
    • Kresge, N.1    Vacquier, V.D.2    Stout, C.D.3
  • 69
    • 56249132454 scopus 로고    scopus 로고
    • The interplay of ligand binding and quaternary structure in the diverse interactions of dynein light chain LC8
    • Benison G., Karplus P.A., Barbar E. The interplay of ligand binding and quaternary structure in the diverse interactions of dynein light chain LC8. J. Mol. Biol. 2008, 384:954-966.
    • (2008) J. Mol. Biol. , vol.384 , pp. 954-966
    • Benison, G.1    Karplus, P.A.2    Barbar, E.3
  • 70
    • 0035852805 scopus 로고    scopus 로고
    • Dimerization and folding of LC8, a highly conserved light chain of cytoplasmic dynein
    • Barbar E., Kleinman B., Imhoff D., Li M., Hays T.S., Hare M. Dimerization and folding of LC8, a highly conserved light chain of cytoplasmic dynein. Biochemistry 2001, 40:1596-1605.
    • (2001) Biochemistry , vol.40 , pp. 1596-1605
    • Barbar, E.1    Kleinman, B.2    Imhoff, D.3    Li, M.4    Hays, T.S.5    Hare, M.6
  • 72
    • 0028102938 scopus 로고
    • Determination of the monomer-dimer equilibrium of interleukin-8 reveals it is a monomer at physiological concentrations
    • Burrows S.D., Doyle M.L., Murphy K.P., Franklin S.G., White J.R., Brooks I., et al. Determination of the monomer-dimer equilibrium of interleukin-8 reveals it is a monomer at physiological concentrations. Biochemistry 1994, 33:12741-12745.
    • (1994) Biochemistry , vol.33 , pp. 12741-12745
    • Burrows, S.D.1    Doyle, M.L.2    Murphy, K.P.3    Franklin, S.G.4    White, J.R.5    Brooks, I.6
  • 74
    • 0032479285 scopus 로고    scopus 로고
    • Refined structure of Cro repressor protein from bacteriophage lambda suggests both flexibility and plasticity
    • Ohlendorf D.H., Tronrud D.E., Matthews B.W. Refined structure of Cro repressor protein from bacteriophage lambda suggests both flexibility and plasticity. J. Mol. Biol. 1998, 280:129-136.
    • (1998) J. Mol. Biol. , vol.280 , pp. 129-136
    • Ohlendorf, D.H.1    Tronrud, D.E.2    Matthews, B.W.3
  • 75
    • 0034687127 scopus 로고    scopus 로고
    • Coupled energetics of lambda cro repressor self-assembly and site-specific DNA operator binding I: analysis of cro dimerization from nanomolar to micromolar concentrations
    • Darling P.J., Holt J.M., Ackers G.K. Coupled energetics of lambda cro repressor self-assembly and site-specific DNA operator binding I: analysis of cro dimerization from nanomolar to micromolar concentrations. Biochemistry 2000, 39:11500-11507.
    • (2000) Biochemistry , vol.39 , pp. 11500-11507
    • Darling, P.J.1    Holt, J.M.2    Ackers, G.K.3
  • 76
    • 0022517026 scopus 로고
    • Ligand-controlled dissociation of Chromatium vinosum cytochrome c'
    • Doyle M.L., Gill S.J., Cusanovich M.A. Ligand-controlled dissociation of Chromatium vinosum cytochrome c'. Biochemistry 1986, 25:2509-2516.
    • (1986) Biochemistry , vol.25 , pp. 2509-2516
    • Doyle, M.L.1    Gill, S.J.2    Cusanovich, M.A.3
  • 77
  • 78
    • 17544403421 scopus 로고    scopus 로고
    • Proteolytic E-cadherin activation followed by solution NMR and X-ray crystallography
    • Häussinger D., Ahrens T., Aberle T., Engel J., Stetefeld J., Grzesiek S. Proteolytic E-cadherin activation followed by solution NMR and X-ray crystallography. EMBO J. 2004, 23:1699-1708.
    • (2004) EMBO J. , vol.23 , pp. 1699-1708
    • Häussinger, D.1    Ahrens, T.2    Aberle, T.3    Engel, J.4    Stetefeld, J.5    Grzesiek, S.6
  • 81
    • 0037388314 scopus 로고    scopus 로고
    • Metal stoichiometry and functional studies of the diphtheria toxin repressor
    • Spiering M.M., Ringe D., Murphy J.R., Marletta M.A. Metal stoichiometry and functional studies of the diphtheria toxin repressor. Proc. Natl Acad. Sci. USA 2003, 100:3808-3813.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 3808-3813
    • Spiering, M.M.1    Ringe, D.2    Murphy, J.R.3    Marletta, M.A.4
  • 82
    • 0029586759 scopus 로고
    • Protein-protein interaction at crystal contacts
    • Janin J., Rodier F. Protein-protein interaction at crystal contacts. Proteins 1995, 23:580-587.
    • (1995) Proteins , vol.23 , pp. 580-587
    • Janin, J.1    Rodier, F.2
  • 83
    • 0037032445 scopus 로고    scopus 로고
    • Pyrococcus furiosus ferredoxin is a functional dimer
    • Hasan M.N., Hagedoorn P.L., Hagen W.R. Pyrococcus furiosus ferredoxin is a functional dimer. FEBS Lett. 2002, 531:335-338.
    • (2002) FEBS Lett. , vol.531 , pp. 335-338
    • Hasan, M.N.1    Hagedoorn, P.L.2    Hagen, W.R.3
  • 85
    • 0028881975 scopus 로고
    • SURFNET: a program for visualizing molecular surfaces, cavities, and intermolecular interactions
    • Laskowski R.A. SURFNET: a program for visualizing molecular surfaces, cavities, and intermolecular interactions. J. Mol. Graph. 1995, 13:323-330.
    • (1995) J. Mol. Graph. , vol.13 , pp. 323-330
    • Laskowski, R.A.1
  • 86
    • 0027772959 scopus 로고
    • Shape complementarity at protein-protein interfaces
    • Lawrence M.C., Colman P.M. Shape complementarity at protein-protein interfaces. J. Mol. Biol. 1993, 234:946-950.
    • (1993) J. Mol. Biol. , vol.234 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 88
    • 0031450506 scopus 로고    scopus 로고
    • Hydrogen bonds and salt bridges across protein-protein interfaces
    • Xu D., Tsai C.J., Nussinov R. Hydrogen bonds and salt bridges across protein-protein interfaces. Protein Eng. 1997, 10:999-1012.
    • (1997) Protein Eng. , vol.10 , pp. 999-1012
    • Xu, D.1    Tsai, C.J.2    Nussinov, R.3
  • 90
    • 0027288463 scopus 로고
    • The HSSP database of protein structure-sequence alignments
    • Sander C., Schneider R. The HSSP database of protein structure-sequence alignments. Nucleic Acids Res. 1993, 21:3105-3109.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 3105-3109
    • Sander, C.1    Schneider, R.2
  • 91
    • 27344440132 scopus 로고    scopus 로고
    • Conservation and relative importance of residues across protein-protein interfaces
    • Guharoy M., Chakrabarti P. Conservation and relative importance of residues across protein-protein interfaces. Proc. Natl Acad. Sci. USA 2005, 102:15447-15452.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 15447-15452
    • Guharoy, M.1    Chakrabarti, P.2
  • 92
    • 0028865843 scopus 로고
    • 3D domain swapping: a mechanism for oligomer assembly
    • Bennett M.J., Schlunegger M.P., Eisenberg D. 3D domain swapping: a mechanism for oligomer assembly. Protein Sci. 1995, 4:2455-2468.
    • (1995) Protein Sci. , vol.4 , pp. 2455-2468
    • Bennett, M.J.1    Schlunegger, M.P.2    Eisenberg, D.3
  • 93
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: as domains continue to swap
    • Liu Y., Eisenberg D. 3D domain swapping: as domains continue to swap. Protein Sci. 2002, 11:1285-1299.
    • (2002) Protein Sci. , vol.11 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 95
    • 0017893796 scopus 로고
    • The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen-pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 Å resolution
    • Bode W., Schwager P., Huber R. The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen-pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 Å resolution. J. Mol. Biol. 1978, 118:99-112.
    • (1978) J. Mol. Biol. , vol.118 , pp. 99-112
    • Bode, W.1    Schwager, P.2    Huber, R.3
  • 98
    • 34548820455 scopus 로고    scopus 로고
    • The crystal structure of human E-cadherin domains 1 and 2, and comparison with other cadherins in the context of adhesion mechanism
    • Parisini E., Higgins J.M., Liu J.H., Brenner M.B., Wang J.H. The crystal structure of human E-cadherin domains 1 and 2, and comparison with other cadherins in the context of adhesion mechanism. J. Mol. Biol. 2007, 373:401-411.
    • (2007) J. Mol. Biol. , vol.373 , pp. 401-411
    • Parisini, E.1    Higgins, J.M.2    Liu, J.H.3    Brenner, M.B.4    Wang, J.H.5
  • 99
    • 0028774535 scopus 로고
    • Old yellow enzyme at 2 Å resolution: overall structure, ligand binding, and comparison with related flavoproteins
    • Fox K.M., Karplus P.A. Old yellow enzyme at 2 Å resolution: overall structure, ligand binding, and comparison with related flavoproteins. Structure 1994, 2:1089-1105.
    • (1994) Structure , vol.2 , pp. 1089-1105
    • Fox, K.M.1    Karplus, P.A.2
  • 100
    • 0035344649 scopus 로고    scopus 로고
    • A dimeric two-component receiver domain inhibits the sigma54-dependent ATPase in DctD
    • Meyer M.G., Park S., Zeringue L., Staley M., McKinstry M., Kaufman R.I., et al. A dimeric two-component receiver domain inhibits the sigma54-dependent ATPase in DctD. FASEB J. 2001, 15:1326-1328.
    • (2001) FASEB J. , vol.15 , pp. 1326-1328
    • Meyer, M.G.1    Park, S.2    Zeringue, L.3    Staley, M.4    McKinstry, M.5    Kaufman, R.I.6
  • 102
    • 2642524483 scopus 로고    scopus 로고
    • A physical reference state unifies the structure-derived potential of mean force for protein folding and binding
    • Liu S., Zhang C., Zhou H., Zhou Y. A physical reference state unifies the structure-derived potential of mean force for protein folding and binding. Proteins 2004, 56:93-101.
    • (2004) Proteins , vol.56 , pp. 93-101
    • Liu, S.1    Zhang, C.2    Zhou, H.3    Zhou, Y.4
  • 104
    • 0033534518 scopus 로고    scopus 로고
    • Evolutionary constraints for dimer formation in prokaryotic Cu,Zn superoxide dismutase
    • Bordo D., Matak D., Djinovic-Carugo K., Rosano C., Pesce A., Bolognesi M., et al. Evolutionary constraints for dimer formation in prokaryotic Cu,Zn superoxide dismutase. J. Mol. Biol. 1999, 285:283-296.
    • (1999) J. Mol. Biol. , vol.285 , pp. 283-296
    • Bordo, D.1    Matak, D.2    Djinovic-Carugo, K.3    Rosano, C.4    Pesce, A.5    Bolognesi, M.6
  • 105
    • 5144232009 scopus 로고    scopus 로고
    • Growth-regulatory human galectin-1: crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding
    • López-Lucendo M.F., Solís D., André S., Hirabayashi J., Kasai K., Kaltner H., et al. Growth-regulatory human galectin-1: crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding. J. Mol. Biol. 2004, 343:957-970.
    • (2004) J. Mol. Biol. , vol.343 , pp. 957-970
    • López-Lucendo, M.F.1    Solís, D.2    André, S.3    Hirabayashi, J.4    Kasai, K.5    Kaltner, H.6
  • 106
    • 36749048724 scopus 로고    scopus 로고
    • Prediction of the structure of symmetrical protein assemblies
    • André I., Bradley P., Wang C., Baker D. Prediction of the structure of symmetrical protein assemblies. Proc. Natl Acad. Sci. USA 2007, 104:17656-17661.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 17656-17661
    • André, I.1    Bradley, P.2    Wang, C.3    Baker, D.4
  • 108
    • 78651189765 scopus 로고
    • On the nature of allosteric transition: a plausible model
    • Monod J., Wyman J., Changeux J.P. On the nature of allosteric transition: a plausible model. J. Mol. Biol. 1965, 12:88-118.
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 109
    • 0004034454 scopus 로고
    • Department of Biochemistry and Molecular Biology, University College of London, London, UK
    • Hubbard S.J. NACCESS: Program for Calculating Accessibilities 1992, Department of Biochemistry and Molecular Biology, University College of London, London, UK.
    • (1992) NACCESS: Program for Calculating Accessibilities
    • Hubbard, S.J.1
  • 110
    • 0015222647 scopus 로고
    • The interpretation of protein structures: estimation of static accessibility
    • Lee B., Richards F.M. The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 1971, 55:379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 111
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald I.K., Thornton J.M. Satisfying hydrogen bonding potential in proteins. J. Mol. Biol. 1994, 238:777-793.
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.