메뉴 건너뛰기




Volumn 60, Issue 1, 2005, Pages 103-109

Crystal packing effects on protein loops

Author keywords

Crystal contacts; Crystal lattice; Crystallography; Loop prediction; NMR; Protein structure

Indexed keywords

PROTEIN;

EID: 19544370676     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20492     Document Type: Article
Times cited : (31)

References (21)
  • 1
    • 0026651557 scopus 로고
    • NMR Structure determination in solution: A critique and comparison with X-ray crystallography
    • Wagner G, Hyberts SG, Havel TF. NMR Structure determination in solution: a critique and comparison with X-ray crystallography. Annu Rev Biophys Biomol Struct 1992;21:167-198.
    • (1992) Annu Rev Biophys Biomol Struct , vol.21 , pp. 167-198
    • Wagner, G.1    Hyberts, S.G.2    Havel, T.F.3
  • 2
    • 0037035520 scopus 로고    scopus 로고
    • The NMR analysis of the monomeric form of a mutant unliganded bovine neurophysin: Comparison with the crystal structure of a neurophysin dimer
    • Nguyen TL, Breslow E. The NMR analysis of the monomeric form of a mutant unliganded bovine neurophysin: comparison with the crystal structure of a neurophysin dimer. Biochemistry 2002;41; 5920-5930.
    • (2002) Biochemistry , vol.41 , pp. 5920-5930
    • Nguyen, T.L.1    Breslow, E.2
  • 3
    • 0036160702 scopus 로고    scopus 로고
    • The NMR solution structure of the isolated Apo Pin1 WW domain: Comparison to the x-ray crystal structures of Pin1
    • Kowalski JA, Liu K, Kelly JW. The NMR solution structure of the isolated Apo Pin1 WW domain: comparison to the x-ray crystal structures of Pin1. Biopolymers 2002;63(2)111-121.
    • (2002) Biopolymers , vol.63 , Issue.2 , pp. 111-121
    • Kowalski, J.A.1    Liu, K.2    Kelly, J.W.3
  • 4
    • 0027980862 scopus 로고
    • Polypeptide conformational space: Dynamics by solution NMR disorder by X-ray crystallography
    • Pascal SM, Cross TA. Polypeptide conformational space: dynamics by solution NMR disorder by X-ray crystallography. J Mol Biol 1994;241:431-439.
    • (1994) J Mol Biol , vol.241 , pp. 431-439
    • Pascal, S.M.1    Cross, T.A.2
  • 6
    • 0026645602 scopus 로고
    • Variability of conformations at crystal contacts in BPTI represent true low energy structures: Correspondence among lattice packing and molecular dynamics structures
    • Kossiakoff AA, Randall M, Guenot J, Eigenbrot C. Variability of conformations at crystal contacts in BPTI represent true low energy structures: correspondence among lattice packing and molecular dynamics structures. Proteins 1992;14:65-74.
    • (1992) Proteins , vol.14 , pp. 65-74
    • Kossiakoff, A.A.1    Randall, M.2    Guenot, J.3    Eigenbrot, C.4
  • 7
    • 19244368728 scopus 로고    scopus 로고
    • Crystal packing induces a conformational change in Prolifin-I from Acanthamoeba castellani
    • Liu S, Fedorov AA, Pollard TD, Lattman EE, Almo S, Magnus K. Crystal packing induces a conformational change in Prolifin-I from Acanthamoeba castellani. J Struct Biol 1998;123:22-29.
    • (1998) J Struct Biol , vol.123 , pp. 22-29
    • Liu, S.1    Fedorov, A.A.2    Pollard, T.D.3    Lattman, E.E.4    Almo, S.5    Magnus, K.6
  • 9
    • 0026740792 scopus 로고
    • Structural effects induced by mutagenesis affected by crystal packing factors: The structure of a 30-51 disulfide mutant of basic pancreatic trypsin inhibitor
    • Eigenbrot C, Randal M, Kossiakoff AA. Structural effects induced by mutagenesis affected by crystal packing factors: The structure of a 30-51 disulfide mutant of basic pancreatic trypsin inhibitor. Proteins 1992;14:75-87.
    • (1992) Proteins , vol.14 , pp. 75-87
    • Eigenbrot, C.1    Randal, M.2    Kossiakoff, A.A.3
  • 10
    • 0032525183 scopus 로고    scopus 로고
    • Packing forces in nine crystal forms of Cutinase
    • Jelsch C, Longhi S, Cambillau C. Packing forces in nine crystal forms of Cutinase. Proteins 1998;31:320-333.
    • (1998) Proteins , vol.31 , pp. 320-333
    • Jelsch, C.1    Longhi, S.2    Cambillau, C.3
  • 11
    • 0029150760 scopus 로고
    • Protein flexibility and adaptability seen in 25 crystal forms of T4 Lysozyme
    • Zhang X, Wozniak JA, Matthews BW. Protein flexibility and adaptability seen in 25 crystal forms of T4 Lysozyme. J Mol Biol 1995;250:527-552.
    • (1995) J Mol Biol , vol.250 , pp. 527-552
    • Zhang, X.1    Wozniak, J.A.2    Matthews, B.W.3
  • 12
    • 0036310711 scopus 로고    scopus 로고
    • On the role of crystal packing forces in determining protein sidechain conformations
    • Jacobson MP, Friesner RA, Xiang Z, Honig B. On the role of crystal packing forces in determining protein sidechain conformations. J Mol Biol 2002;320:597-608.
    • (2002) J Mol Biol , vol.320 , pp. 597-608
    • Jacobson, M.P.1    Friesner, R.A.2    Xiang, Z.3    Honig, B.4
  • 14
    • 1442277682 scopus 로고    scopus 로고
    • Computational modeling of the catalytic reaction in triosephosphate isomerase
    • Gallar V, Jacobson MP, Mcdermott A, Friesner RA. Computational modeling of the catalytic reaction in triosephosphate isomerase. J Mol Biol 2004;37:227-239.
    • (2004) J Mol Biol , vol.37 , pp. 227-239
    • Gallar, V.1    Jacobson, M.P.2    Mcdermott, A.3    Friesner, R.A.4
  • 15
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids
    • Jorgensen WL, Maxwell DS, Tirado-Rives J. Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids. J Am Chem Soc 1996;118: 11225-11236.
    • (1996) J Am Chem Soc , vol.118 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 16
    • 0035913529 scopus 로고    scopus 로고
    • Evaluation and reparameterization of the OPLS-AA force field for protein via comparison with accurate quantum mechanical calculations on peptides
    • Kaminski GA, Friesner RA, Tirado-Rives J, Jorgensen, WL. Evaluation and reparameterization of the OPLS-AA force field for protein via comparison with accurate quantum mechanical calculations on peptides. J Phys Chem B 2001;105(28):6474-6487.
    • (2001) J Phys Chem B , vol.105 , Issue.28 , pp. 6474-6487
    • Kaminski, G.A.1    Friesner, R.A.2    Tirado-Rives, J.3    Jorgensen, W.L.4
  • 18
    • 0001246294 scopus 로고    scopus 로고
    • Generalized Born model based on a surface integral formulation
    • Ghosh A, Rapp C, Friesner RA. Generalized Born model based on a surface integral formulation. J Phys Chem B 1998;102:10983-10990.
    • (1998) J Phys Chem B , vol.102 , pp. 10983-10990
    • Ghosh, A.1    Rapp, C.2    Friesner, R.A.3
  • 19
    • 0033810049 scopus 로고    scopus 로고
    • Modeling of loops in protein structures
    • Fiser A, Do RKG, Sali A. Modeling of loops in protein structures. Protein Sci 2000;9:1753-1773.
    • (2000) Protein Sci , vol.9 , pp. 1753-1773
    • Fiser, A.1    Do, R.K.G.2    Sali, A.3
  • 20
    • 0033452738 scopus 로고    scopus 로고
    • Exploring the conformational diversity of loops on conserved frameworks
    • Li W, Liang S, Wang R, Lai L, Han Y. Exploring the conformational diversity of loops on conserved frameworks. Protein Eng 1999;12:1075-1086.
    • (1999) Protein Eng , vol.12 , pp. 1075-1086
    • Li, W.1    Liang, S.2    Wang, R.3    Lai, L.4    Han, Y.5
  • 21
    • 0036675042 scopus 로고    scopus 로고
    • Structure-based design of a novel peptide inhibitor of HIV-1 Integrase: A computer modeling approach
    • Rao SR, Bhatnagar S, Ahuja V. Structure-based design of a novel peptide inhibitor of HIV-1 Integrase: a computer modeling approach. J Biomol Struct Dyn 2002;20:31-38.
    • (2002) J Biomol Struct Dyn , vol.20 , pp. 31-38
    • Rao, S.R.1    Bhatnagar, S.2    Ahuja, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.