Data

Crystal structure of the HIV-1 integrase core domain to 1.4A (PDB ID 3L3U): data

Monash University
Dr David Chalmers (Aggregated by) Dr Martin Scanlon (Associated with)
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ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Adc&rfr_id=info%3Asid%2FANDS&rft_id=1959.1/470432&rft.title=Crystal structure of the HIV-1 integrase core domain to 1.4A (PDB ID 3L3U): data&rft.identifier=1959.1/470432&rft.publisher=Monash University&rft.description=This data collection represents the highest resolution crystal structure of the IN core domain to date, and also presents a crystal structure of the IN core domain in complex with sucrose which is bound at the dimer interface in a region that has previously been reported to bind integrase inhibitors. HIV integrase (IN) is an essential enzyme in HIV replication and an important target for drug design. IN has been shown to interact with a number of cellular and viral proteins during the integration process. Disruption of these important interactions could provide a mechanism for allosteric inhibition of IN.&rft.creator=Dr David Chalmers&rft.date=2012&rft.relation=10.1016/j.febslet.2010.03.016&rft.relation=10.1007/s10822-005-5256-2&rft.relation=10.1002/cmdc.201000483&rft_subject=Biologically Active Molecules&rft_subject=CHEMICAL SCIENCES&rft_subject=MEDICINAL AND BIOMOLECULAR CHEMISTRY&rft_subject=Biomolecular Modelling and Design&rft_subject=Characterisation of Biological Macromolecules&rft_subject=Virology&rft_subject=BIOLOGICAL SCIENCES&rft_subject=MICROBIOLOGY&rft_subject=Human immunodeficiency virus&rft_subject=HIV&rft_subject=HIV integrase&rft_subject=HIV-1&rft_subject=Acquired immune deficiency syndrome&rft_subject=AIDS&rft_subject=Drug discovery&rft_subject=Protein structure&rft_subject=Virus replication&rft_subject=Allosteric regulation&rft_subject=Binding sites&rft_subject=Crystallography&rft_subject=X-Ray&rft_subject=Glycerol&rft_subject=Models&rft_subject=Protein binding&rft_subject=Protein multimerization&rft_subject=Sucrose&rft_subject=HIV integrase inhibitors&rft.type=dataset&rft.language=English Access the data
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This data collection represents the highest resolution crystal structure of the IN core domain to date, and also presents a crystal structure of the IN core domain in complex with sucrose which is bound at the dimer interface in a region that has previously been reported to bind integrase inhibitors. HIV integrase (IN) is an essential enzyme in HIV replication and an important target for drug design. IN has been shown to interact with a number of cellular and viral proteins during the integration process. Disruption of these important interactions could provide a mechanism for allosteric inhibition of IN.

Notes

PDB deposit package contains: FASTA Sequence, PDB File (Text), PDB File (gz), mmCIF File, mmCIF File (gz), PDBML/XML File PDBML/XML File (gz), Structure Factor (Text), Structure Factor (gz), Biological Assembly (gz) (A+S).

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Subjects
AIDS | Acquired immune deficiency syndrome | Allosteric regulation | Biological Sciences | Binding sites | Biologically Active Molecules | Biomolecular Modelling and Design | Chemical Sciences | Characterisation of Biological Macromolecules | Crystallography | Drug discovery | Glycerol | HIV | HIV integrase | HIV integrase inhibitors | HIV-1 | Human immunodeficiency virus | Medicinal and Biomolecular Chemistry | Microbiology | Models | Protein binding | Protein multimerization | Protein structure | Sucrose | Virology | Virus replication | X-Ray |

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