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(→Recognition of HIV TAR RNA by peptide mimetic of Tat protein)
Current revision (20:20, 19 December 2012) (edit) (undo)
 
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<StructureSection load='2kx5' size='350' side='right' caption= '2KX5' scene=''>
<StructureSection load='2kx5' size='350' side='right' caption= '2KX5' scene=''>
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The pharmacological disruption of the interaction between the HIV Tat protein and its cognate transactivation response RNA (TAR) would generate novel anti-viral drugs with a low susceptibility to drug resistance, but efforts to discover ligands with sufficient potency to warrant pharmaceutical development have been unsuccessful<ref>PMID1245</ref>. We have previously described a family of structurally constrained ?-hairpin peptides that potently inhibits viral growth in HIV-infected cells. The nuclear magnetic resonance (NMR) structure of an inhibitory complex revealed that the peptide makes intimate contacts with the 3-nt bulge and the upper helix of the RNA hairpin, but that a single residue contacts the apical loop where recruitment of the essential cellular co-factor cyclin T? occurs. Attempting to extend the peptide to form more interactions with the RNA loop, we examined a library of longer peptides and achieved > 6-fold improvement in affinity. The structure of TAR bound to one of the extended peptides reveals that the peptide slides down the major groove of the RNA, relative to our design, in order to maintain critical interactions with TAR. These conserved contacts involve three amino acid side chains and identify critical interaction points required for potent and specific binding to TAR RNA. They constitute a template of essential interactions required for inhibition of this RNA.<ref>DOI 1234</ref>
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{{ABSTRACT_PUBMED_20724442}}
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</StructureSection>
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Non-canonical interactions are important for expand mayor groove duplex
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Ja Ja Ja<ref>PMID 9322034</ref>
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</StructureSection>
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<scene name='Sandbox_UC_23/Triplet/1'>Triplets1</scene>
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==Your Heading Here (maybe something like 'Structure')==<StructureSection load='2kx5' size='500' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[2kx5]])' scene='Sandbox_UC_23/Triplet/1'>Non-canonical interactions are really important for expand major groove, and it allows the peptide to be inserted. In this triplet, canonical base pair is generated by A27-U38 and non-canonical interaction by Watson Crick edge of U23 and Hoogsteen edge of A27.</StructureSection>
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<references/>

Current revision

Recognition of HIV TAR RNA by peptide mimetic of Tat protein

2KX5

Drag the structure with the mouse to rotate

==Your Heading Here (maybe something like 'Structure')==

Structure of HMG-CoA reductase (PDB entry 2kx5)

Drag the structure with the mouse to rotate
  1. ↑ Melo F, Devos D, Depiereux E, Feytmans E. ANOLEA: a www server to assess protein structures. Proc Int Conf Intell Syst Mol Biol. 1997;5:187-90. PMID:9322034
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