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Volumn 63, Issue 4, 2006, Pages 1112-1118

Crystal structure of TM1367 from Thermotoga maritima at 1.90 Å resolution reveals an atypical member of the cyclophilin (peptidylprolyl isomerase) fold

(48)  Jin, Kevin Kai a,b   Sri Krishna, S a,c   Schwarzenbacher, Robert a,c   McMullan, Daniel a,d   Abdubek, Polat a,d   Agarwalla, Sanjay a,d   Ambing, Eileen a,d   Axelrod, Herbert a,b   Canaves, Jaume M a,c   Chiu, Hsiu Ju a,b   Deacon, Ashley M a,b   DiDonato, Michael a,d   Elsliger, Marc André a,e   Feuerhelm, Julie a,d   Godzik, Adam a,c   Grittini, Carina a,e   Grzechnik, Slawomir K a,c   Hale, Joanna a,d   Hampton, Eric a,d   Haugen, Justin a,d   more..


Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; CYCLOPHILIN; GENE PRODUCT; PROTEIN TM1367; UNCLASSIFIED DRUG;

EID: 33646808580     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.20894     Document Type: Article
Times cited : (7)

References (29)
  • 5
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews BW. Solvent content of protein crystals. J Mol Biol 1968;33:491-497.
    • (1968) J Mol Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 6
    • 3242886389 scopus 로고    scopus 로고
    • MOLPROBITY: Structure validation and all-atom contact analysis for nucleic acids and their complexes
    • Davis IW, Murray LW, Richardson JS, Richardson DC. MOLPROBITY: structure validation and all-atom contact analysis for nucleic acids and their complexes. Nucleic Acids Res 2004;32: W615-619.
    • (2004) Nucleic Acids Res , vol.32
    • Davis, I.W.1    Murray, L.W.2    Richardson, J.S.3    Richardson, D.C.4
  • 8
    • 0028871926 scopus 로고
    • Dali: A network tool for protein structure comparison
    • Holm L, Sander C. Dali: a network tool for protein structure comparison. Trends Biochem Sci 1995;20:478-480.
    • (1995) Trends Biochem Sci , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 9
    • 0033736147 scopus 로고    scopus 로고
    • Immunophilins: Switched on protein binding domains?
    • Ivery MT. Immunophilins: switched on protein binding domains? Med Res Rev 2000;20:452-484.
    • (2000) Med Res Rev , vol.20 , pp. 452-484
    • Ivery, M.T.1
  • 10
    • 0029970349 scopus 로고    scopus 로고
    • The substrate-binding site in Escherichia coli cyclophilin a preferably recognizes a cis-proline isomer or a highly distorted form of the trans isomer
    • Konno M, Ito M, Hayano T, Takahashi N. The substrate-binding site in Escherichia coli cyclophilin A preferably recognizes a cis-proline isomer or a highly distorted form of the trans isomer. J Mol Biol 1996;256:897-908.
    • (1996) J Mol Biol , vol.256 , pp. 897-908
    • Konno, M.1    Ito, M.2    Hayano, T.3    Takahashi, N.4
  • 12
    • 0032970430 scopus 로고    scopus 로고
    • A proposed molecular model for the interaction of calcineurin with the cyclosporin A-cyclophilin a complex
    • Ivery MT. A proposed molecular model for the interaction of calcineurin with the cyclosporin A-cyclophilin A complex. Bioorg Med Chem 1999;7:1389-1402.
    • (1999) Bioorg Med Chem , vol.7 , pp. 1389-1402
    • Ivery, M.T.1
  • 13
    • 0027071803 scopus 로고
    • Active site mutants of human cyclophilin a separate peptidyl-prolyl isomerase activity from cyclosporin a binding and calcineurin inhibition
    • Zydowsky LD, Etzkorn FA, Chang HY, Ferguson SB, Stolz LA, Ho SI, Walsh CT. Active site mutants of human cyclophilin A separate peptidyl-prolyl isomerase activity from cyclosporin A binding and calcineurin inhibition. Protein Sci 1992;1:1092-1099.
    • (1992) Protein Sci , vol.1 , pp. 1092-1099
    • Zydowsky, L.D.1    Etzkorn, F.A.2    Chang, H.Y.3    Ferguson, S.B.4    Stolz, L.A.5    Ho, S.I.6    Walsh, C.T.7
  • 14
    • 0037126026 scopus 로고    scopus 로고
    • Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes
    • Huai Q, Kim HY, Liu Y, Zhao Y, Mondragon A, Liu JO, Ke H. Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes. Proc Natl Acad Sci USA 2002;99:12037-12042.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 12037-12042
    • Huai, Q.1    Kim, H.Y.2    Liu, Y.3    Zhao, Y.4    Mondragon, A.5    Liu, J.O.6    Ke, H.7
  • 16
    • 0027363385 scopus 로고
    • Peptidylproline cis-trans-isomerases: Immunophilins
    • Galat A. Peptidylproline cis-trans-isomerases: immunophilins. Eur J Biochem 1993;216:689-707.
    • (1993) Eur J Biochem , vol.216 , pp. 689-707
    • Galat, A.1
  • 17
    • 0032169688 scopus 로고    scopus 로고
    • PQS: A protein quaternary structure file server
    • Henrick K, Thornton JM. 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
  • 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
    • 0032104477 scopus 로고    scopus 로고
    • How far divergent evolution goes in proteins
    • Murzin AG. How far divergent evolution goes in proteins. Curr Opin Struct Biol 1998;8:380-387.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 380-387
    • Murzin, A.G.1
  • 23
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994;50:760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 25
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 1991;47:110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 27
    • 0032922193 scopus 로고    scopus 로고
    • SFCHKCK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • Vaguine AA, Richelle J, Wodak SJ. SFCHKCK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Crystallogr D Biol Crystallogr 1999;55:191-205.
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 28
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend G. WHAT IF: a molecular modeling and drug design program. J Mol Graph 1990;8:52-56, 29.
    • (1990) J Mol Graph , vol.8 , pp. 52-56
    • Vriend, G.1
  • 29
    • 0032031476 scopus 로고    scopus 로고
    • Error estimates of protein structure coordinates and deviations from standard geometry by full-matrix refinement of gammaB- and betaB2-crystallin
    • Tickle IJ, Laskowski RA, Moss DS. Error estimates of protein structure coordinates and deviations from standard geometry by full-matrix refinement of gammaB- and betaB2-crystallin. Acta Crystallogr D Biol Crystallogr 1998;54:243-252.
    • (1998) Acta Crystallogr D Biol Crystallogr , vol.54 , pp. 243-252
    • Tickle, I.J.1    Laskowski, R.A.2    Moss, D.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.