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Volumn 53, Issue SUPPL. 6, 2003, Pages 340-351

CASP5 Target Classification

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; CONFERENCE PAPER; EVOLUTION; GENOMICS; HUMAN; MOLECULAR MODEL; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY; STRUCTURE ANALYSIS;

EID: 0242267514     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10555     Document Type: Conference Paper
Times cited : (23)

References (31)
  • 1
    • 0032563298 scopus 로고    scopus 로고
    • Conformational variability in structures of the nitrogenase iron proteins from Azotobacter vinelandii and Clostridium pasteurianum
    • Schlessman JL, Woo D, Joshua-Tor L, Howard JB, Rees DC. Conformational variability in structures of the nitrogenase iron proteins from Azotobacter vinelandii and Clostridium pasteurianum. J Mol Biol 1998;280:669-685.
    • (1998) J Mol Biol , vol.280 , pp. 669-685
    • Schlessman, J.L.1    Woo, D.2    Joshua-Tor, L.3    Howard, J.B.4    Rees, D.C.5
  • 2
    • 0026534155 scopus 로고
    • Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0-A resolution
    • Herzberg O, Reddy P, Sutrina S, Saier MH Jr, Reizer J, Kapadia G. Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0-A resolution. Proc Natl Acad Sci USA 1992;89:2499-2503.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2499-2503
    • Herzberg, O.1    Reddy, P.2    Sutrina, S.3    Saier M.H., Jr.4    Reizer, J.5    Kapadia, G.6
  • 3
    • 0035979715 scopus 로고    scopus 로고
    • Structural insights into the ligand binding domains of membrane bound guanylyl cyclases and natriuretic peptide receptors
    • van den Akker F. Structural insights into the ligand binding domains of membrane bound guanylyl cyclases and natriuretic peptide receptors. J Mol Biol 2001;311:923-937.
    • (2001) J Mol Biol , vol.311 , pp. 923-937
    • Van den Akker, F.1
  • 4
    • 0033617457 scopus 로고    scopus 로고
    • The structural basis of ordered substrate binding by serotonin N-acetyltransferase: Enzyme complex at 1.8 A resolution with a bisubstrate analog
    • Hickman AB, Namboodiri MA, Klein DC, Dyda F. The structural basis of ordered substrate binding by serotonin N-acetyltransferase: enzyme complex at 1.8 A resolution with a bisubstrate analog. Cell 1999;97:361-369.
    • (1999) Cell , vol.97 , pp. 361-369
    • Hickman, A.B.1    Namboodiri, M.A.2    Klein, D.C.3    Dyda, F.4
  • 5
    • 0033579559 scopus 로고    scopus 로고
    • Crystal structure of the histone acetyltransferase Hpa2: A tetrameric member of the Gcn5-related N-acetyltransferase superfamily
    • Angus-Hill ML, Dutnall RN, Tafrov ST, Sternglanz R, Ramakrishnan V. Crystal structure of the histone acetyltransferase Hpa2: a tetrameric member of the Gcn5-related N-acetyltransferase superfamily. J Mol Biol 1999;294:1311-1325.
    • (1999) J Mol Biol , vol.294 , pp. 1311-1325
    • Angus-Hill, M.L.1    Dutnall, R.N.2    Tafrov, S.T.3    Sternglanz, R.4    Ramakrishnan, V.5
  • 6
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin AG, Brenner SE, Hubbard T, Chothia C. SCOP: a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 1995;247:536-540.
    • (1995) J Mol Biol , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 10
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L, Sander C. Protein structure comparison by alignment of distance matrices. J Mol Biol 1993;233:123-138.
    • (1993) J Mol Biol , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 11
    • 0033824470 scopus 로고    scopus 로고
    • DaliLite workbench for protein structure comparison
    • Holm L, Park J. DaliLite workbench for protein structure comparison. Bioinformatics 2000;16:566-567.
    • (2000) Bioinformatics , vol.16 , pp. 566-567
    • Holm, L.1    Park, J.2
  • 12
    • 0028223308 scopus 로고
    • The structure of bacteriophage T7 lysozyme, a zinc amidase and an inhibitor of T7 RNA polymerase
    • Cheng X, Zhang X, Pflugrath JW, Studier FW. The structure of bacteriophage T7 lysozyme, a zinc amidase and an inhibitor of T7 RNA polymerase. Proc Natl Acad Sci USA 1994;91:4034-4038.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4034-4038
    • Cheng, X.1    Zhang, X.2    Pflugrath, J.W.3    Studier, F.W.4
  • 14
    • 0030772385 scopus 로고    scopus 로고
    • Crystal structure of murine/human Ubc9 provides insight into the variability of the ubiquitin-conjugating system
    • Tong H, Hateboer G, Perrakis A, Bernards R, Sixma TK. Crystal structure of murine/human Ubc9 provides insight into the variability of the ubiquitin-conjugating system. J Biol Chem 1997;272: 21381-21387.
    • (1997) J Biol Chem , vol.272 , pp. 21381-21387
    • Tong, H.1    Hateboer, G.2    Perrakis, A.3    Bernards, R.4    Sixma, T.K.5
  • 15
    • 0027428548 scopus 로고
    • Evolution of an enzyme activity: Crystallographic structure at 2-A resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase
    • Lobkovsky E, Moews PC, Liu H, Zhao H, Frere JM, Knox JR. Evolution of an enzyme activity: crystallographic structure at 2-A resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase. Proc Natl Acad Sci USA 1993;90:11257-11261.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11257-11261
    • Lobkovsky, E.1    Moews, P.C.2    Liu, H.3    Zhao, H.4    Frere, J.M.5    Knox, J.R.6
  • 16
    • 0028806595 scopus 로고
    • The refined crystallographic structure of a DD-peptidase penicillin-target enzyme at 1.6 A resolution
    • Kelly JA, Kuzin AP. The refined crystallographic structure of a DD-peptidase penicillin-target enzyme at 1.6 A resolution. J Mol Biol 1995;254:223-236.
    • (1995) J Mol Biol , vol.254 , pp. 223-236
    • Kelly, J.A.1    Kuzin, A.P.2
  • 17
    • 0036180211 scopus 로고    scopus 로고
    • EstB from Burkholderia gladioli: A novel esterase with a beta-lactamase fold reveals steric factors to discriminate between esterolytic and beta-lactam cleaving activity
    • Wagner UG, Petersen EI, Schwab H, Kratky C. EstB from Burkholderia gladioli: a novel esterase with a beta-lactamase fold reveals steric factors to discriminate between esterolytic and beta-lactam cleaving activity. Protein Sci 2002;11:467-478.
    • (2002) Protein Sci , vol.11 , pp. 467-478
    • Wagner, U.G.1    Petersen, E.I.2    Schwab, H.3    Kratky, C.4
  • 18
    • 0037195119 scopus 로고    scopus 로고
    • Expanding protein universe and its origin from the biological Big Bang
    • Dokholyan NV, Shakhnovich B, Shakhnovich EI. Expanding protein universe and its origin from the biological Big Bang. Proc Natl Acad Sci USA 2002;99:14132-14136.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14132-14136
    • Dokholyan, N.V.1    Shakhnovich, B.2    Shakhnovich, E.I.3
  • 19
    • 0033529768 scopus 로고    scopus 로고
    • Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly
    • Traub LM, Downs MA, Westrich JL, Fremont DH. Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly. Proc Natl Acad Sci USA 1999;96:8907-8912.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8907-8912
    • Traub, L.M.1    Downs, M.A.2    Westrich, J.L.3    Fremont, D.H.4
  • 20
    • 0037124052 scopus 로고    scopus 로고
    • The structure of a binary complex between a mammalian mevalonate kinase and ATP: Insights into the reaction mechanism and human inherited disease
    • Fu Z, Wang M, Potter D, Miziorko HM, Kim JJ. The structure of a binary complex between a mammalian mevalonate kinase and ATP: insights into the reaction mechanism and human inherited disease. J Biol Chem 2002; 277:18134-18142.
    • (2002) J Biol Chem , vol.277 , pp. 18134-18142
    • Fu, Z.1    Wang, M.2    Potter, D.3    Miziorko, H.M.4    Kim, J.J.5
  • 21
    • 0036174746 scopus 로고    scopus 로고
    • Evidence of intradomain and interdomain flexibility in an OmpR/PhoB homolog from Thermotoga maritima
    • Buckler DR, Zhou Y, Stock AM. Evidence of intradomain and interdomain flexibility in an OmpR/PhoB homolog from Thermotoga maritima. Structure (Camb) 2002;10:153-164.
    • (2002) Structure (Camb) , vol.10 , pp. 153-164
    • Buckler, D.R.1    Zhou, Y.2    Stock, A.M.3
  • 23
    • 0028120546 scopus 로고
    • Atomic structure of the RuvC resolvase: A holliday junction-specific endonuclease from E. coli
    • Ariyoshi M, Vassylyev DG, Iwasaki H, Nakamura H, Shinagawa H, Morikawa K. Atomic structure of the RuvC resolvase: a holliday junction-specific endonuclease from E. coli. Cell 1994;78: 1063-1072.
    • (1994) Cell , vol.78 , pp. 1063-1072
    • Ariyoshi, M.1    Vassylyev, D.G.2    Iwasaki, H.3    Nakamura, H.4    Shinagawa, H.5    Morikawa, K.6
  • 24
    • 0034664813 scopus 로고    scopus 로고
    • SURVEY and SUMMARY: Holliday junction resolvases and related nucleases: Identification of new families, phyletic distribution and evolutionary trajectories
    • Aravind L, Makarova KS, Koonin EV. SURVEY AND SUMMARY: holliday junction resolvases and related nucleases: identification of new families, phyletic distribution and evolutionary trajectories. Nucleic Acids Res 2000;28:3417-3432.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3417-3432
    • Aravind, L.1    Makarova, K.S.2    Koonin, E.V.3
  • 25
    • 0032529457 scopus 로고    scopus 로고
    • Phosphoesterase domains associated with DNA polymerases of diverse origins
    • Aravind L, Koonin EV. Phosphoesterase domains associated with DNA polymerases of diverse origins. Nucleic Acids Res 1998;26: 3746-3752.
    • (1998) Nucleic Acids Res , vol.26 , pp. 3746-3752
    • Aravind, L.1    Koonin, E.V.2
  • 27
    • 0031849756 scopus 로고    scopus 로고
    • The X-ray structure of a cobalamin biosynthetic enzyme, cobalt-precorrin-4 methyltransferase
    • Schubert HL, Wilson KS, Raux E, Woodcock SC, Warren MJ. The X-ray structure of a cobalamin biosynthetic enzyme, cobalt-precorrin-4 methyltransferase. Nat Struct Biol 1998;5:585-592.
    • (1998) Nat Struct Biol , vol.5 , pp. 585-592
    • Schubert, H.L.1    Wilson, K.S.2    Raux, E.3    Woodcock, S.C.4    Warren, M.J.5
  • 28
    • 0034006028 scopus 로고    scopus 로고
    • Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases
    • DeLaBarre B, Thompson PR, Wright GD, Berghuis AM. Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases. Nat Struct Biol 2000;7:238-244.
    • (2000) Nat Struct Biol , vol.7 , pp. 238-244
    • DeLaBarre, B.1    Thompson, P.R.2    Wright, G.D.3    Berghuis, A.M.4
  • 29
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 1997;90:65-75.
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 31
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf RM. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J Mol Graph Model 1997;15:132-134, 112-113.
    • (1997) J Mol Graph Model , vol.15 , pp. 132-134
    • Esnouf, R.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.