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Volumn 5, Issue 7, 2014, Pages 727-729

Protein-ligand cocrystal structures: We can do better

Author keywords

bound ligand strain; Protein ligand cocrystal; structure refinement; structure based design; structure induced fit

Indexed keywords

LIGAND; PROTEIN; PROTEIN BAD;

EID: 84904339885     PISSN: None     EISSN: 19485875     Source Type: Journal    
DOI: 10.1021/ml500220a     Document Type: Review
Times cited : (33)

References (10)
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    • Davis, A. M.; Teague, S. J.; Kleywegt, G. J. Application and limitations of X-ray crystallographic data in structure-based ligand and drug design Angew. Chem., Int. Ed. 2003, 42, 2718-2736
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    • Davis, A.M.1    Teague, S.J.2    Kleywegt, G.J.3
  • 3
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    • Liebeschuetz, J.; Hennemann, J.; Olsson, T.; Groom, C. R. The good, the bad and the twisted: a survey of ligand geometry in protein crystal structures J. Comput.-Aided Mol. Des. 2012, 26, 169-83
    • (2012) J. Comput.-Aided Mol. Des. , vol.26 , pp. 169-183
    • Liebeschuetz, J.1    Hennemann, J.2    Olsson, T.3    Groom, C.R.4
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    • 2342586724 scopus 로고    scopus 로고
    • Conformational analysis of drug-like molecules bound to proteins: An extensive study of ligand reorganization upon binding
    • Perola, E.; Charifson, P. S. Conformational analysis of drug-like molecules bound to proteins: an extensive study of ligand reorganization upon binding J. Med. Chem. 2004, 47, 2499-510
    • (2004) J. Med. Chem. , vol.47 , pp. 2499-2510
    • Perola, E.1    Charifson, P.S.2
  • 6
    • 84900395603 scopus 로고    scopus 로고
    • Accurate macromolecular crystallographic refinement: Incorporation of the linear scaling, semiempirical quantum-mechanics program DivCon into the PHENIX refinement package
    • Borbulevych, O. Y.; Plumley, J. A.; Martin, R. M.; Merz, J.; Kenneth, M.; Westerhoff, L. M. Accurate macromolecular crystallographic refinement: incorporation of the linear scaling, semiempirical quantum-mechanics program DivCon into the PHENIX refinement package Acta Crystallogr., Sect. D: Biol. Crystallogr. 2014, D70, 1-15
    • (2014) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.70 , pp. 1-15
    • Borbulevych, O.Y.1    Plumley, J.A.2    Martin, R.M.3    Merz, J.4    Kenneth, M.5    Westerhoff, L.M.6
  • 7
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R. A.; Huber, R. Accurate bond and angle parameters for X-ray protein structure refinement Acta Crystallogr., Sect. A: Found. Crystallogr. 1991, 47, 392-400
    • (1991) Acta Crystallogr., Sect. A: Found. Crystallogr. , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 8
    • 84864882089 scopus 로고    scopus 로고
    • Significant reduction in errors associated with nonbonded contacts in protein crystal structures: Automated all-atom refinement with PrimeX
    • Bell, J. A.; Ho, K. L.; Farid, R. Significant reduction in errors associated with nonbonded contacts in protein crystal structures: automated all-atom refinement with PrimeX Acta Crystallogr., Sect. D: Biol. Crystallogr. 2012, 68, 935-52
    • (2012) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.68 , pp. 935-952
    • Bell, J.A.1    Ho, K.L.2    Farid, R.3
  • 9
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    • Reintroducing electrostatics into macromolecular crystallographic refinement: Application to neutron crystallography and DNA hydration
    • Fenn, T. D.; Schnieders, M. J.; Mustyakimov, M.; Wu, C.; Langan, P.; Pande, V. S.; Brunger, A. T. Reintroducing electrostatics into macromolecular crystallographic refinement: application to neutron crystallography and DNA hydration Structure 2011, 19, 523-33
    • (2011) Structure , vol.19 , pp. 523-533
    • Fenn, T.D.1    Schnieders, M.J.2    Mustyakimov, M.3    Wu, C.4    Langan, P.5    Pande, V.S.6    Brunger, A.T.7
  • 10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.