Rapid Protein–Ligand Costructures from Sparse NOE Data
An efficient way to rapidly generate protein–ligand costructures based on solution-NMR using sparse NOE data combined with selective isotope labeling is presented. A docked model of the 27 kDa N-terminal ATPase domain of Hsp90 bound to a small molecule ligand was generated using only 21 intermolecul...
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| Veröffentlicht in: | Journal of medicinal chemistry 2012-12, Vol.55 (23), p.10786-10790 |
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| container_end_page | 10790 |
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| container_issue | 23 |
| container_start_page | 10786 |
| container_title | Journal of medicinal chemistry |
| container_volume | 55 |
| creator | Shah, Dipen M. AB, Eiso Diercks, Tammo Hass, Mathias A. S. van Nuland, Nico A. J. Siegal, Gregg |
| description | An efficient way to rapidly generate protein–ligand costructures based on solution-NMR using sparse NOE data combined with selective isotope labeling is presented. A docked model of the 27 kDa N-terminal ATPase domain of Hsp90 bound to a small molecule ligand was generated using only 21 intermolecular NOEs, which uniquely defined both the binding site and the orientation of the ligand. The approach can prove valuable for the early stages of fragment-based drug discovery. |
| doi_str_mv | 10.1021/jm301396d |
| format | Article |
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The approach can prove valuable for the early stages of fragment-based drug discovery.</description><subject>Adenosine Triphosphatases - metabolism</subject><subject>HSP90 Heat-Shock Proteins - metabolism</subject><subject>Ligands</subject><subject>Nuclear Magnetic Resonance, Biomolecular - methods</subject><subject>Proteins - chemistry</subject><issn>0022-2623</issn><issn>1520-4804</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkLlOw0AURUcIREKg4AeQGyQoDG82LyUKYZEigljq0XgW5Cj2mBm7oOMf-EO-hEEJqahec965uhehYwwXGAi-XDYUMC0zvYPGmBNIWQFsF40BCElJRugIHYSwBACKCd1HI0Ix43lJxqh4kl2tk0fvelO3359f8_pNtjqZutD7QfWDNyGx3jXJcyd9MMnDYpZcy14eoj0rV8Ecbe4Evd7MXqZ36Xxxez-9mqeSYt6nhcyBVFhZwFxzyrMYrGVe8YzllpUsV1WlNLXAFMNVwSlRYJk18Q1yYCWdoLO1t_PufTChF00dlFmtZGvcEEQsVAIvMWQRPV-jyrsQvLGi83Uj_YfAIH6HEtuhInuy0Q5VY_SW_FsmAqdrQKoglm7wbWz5j-gH1G5tog</recordid><startdate>20121213</startdate><enddate>20121213</enddate><creator>Shah, Dipen M.</creator><creator>AB, Eiso</creator><creator>Diercks, Tammo</creator><creator>Hass, Mathias A. 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| ispartof | Journal of medicinal chemistry, 2012-12, Vol.55 (23), p.10786-10790 |
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| language | eng |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | Adenosine Triphosphatases - metabolism HSP90 Heat-Shock Proteins - metabolism Ligands Nuclear Magnetic Resonance, Biomolecular - methods Proteins - chemistry |
| title | Rapid Protein–Ligand Costructures from Sparse NOE Data |
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