1z9e: Difference between revisions

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[[Image:1z9e.gif|left|200px]]<br />
[[Image:1z9e.gif|left|200px]]<br /><applet load="1z9e" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1z9e" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1z9e" />
caption="1z9e" />
'''Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75'''<br />
'''Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75'''<br />


==Overview==
==Overview==
Lens epithelium-derived growth factor (LEDGF)/p75 is the dominant binding, partner of HIV-1 integrase (IN) in human cells. We have determined the NMR, structure of the integrase-binding domain (IBD) in LEDGF and identified, amino acid residues essential for the interaction. The IBD is a compact, right-handed bundle composed of five alpha-helices. Based on folding, topology, the IBD is structurally related to a diverse family of, alpha-helical proteins that includes eukaryotic translation initiation, factor eIF4G and karyopherin-beta. LEDGF residues essential for the, interaction with IN were localized to interhelical loop regions of the, bundle structure. Interaction-defective IN mutants were previously shown, to cripple replication although they retained catalytic function. The, initial structure determination of a host cell factor that tightly binds, to a retroviral enzyme lays the groundwork for understanding enzyme-host, interactions important for viral replication.
Lens epithelium-derived growth factor (LEDGF)/p75 is the dominant binding partner of HIV-1 integrase (IN) in human cells. We have determined the NMR structure of the integrase-binding domain (IBD) in LEDGF and identified amino acid residues essential for the interaction. The IBD is a compact right-handed bundle composed of five alpha-helices. Based on folding topology, the IBD is structurally related to a diverse family of alpha-helical proteins that includes eukaryotic translation initiation factor eIF4G and karyopherin-beta. LEDGF residues essential for the interaction with IN were localized to interhelical loop regions of the bundle structure. Interaction-defective IN mutants were previously shown to cripple replication although they retained catalytic function. The initial structure determination of a host cell factor that tightly binds to a retroviral enzyme lays the groundwork for understanding enzyme-host interactions important for viral replication.


==About this Structure==
==About this Structure==
1Z9E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z9E OCA].  
1Z9E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z9E OCA].  


==Reference==
==Reference==
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[[Category: Maertens, G.]]
[[Category: Maertens, G.]]
[[Category: Rahman, S.]]
[[Category: Rahman, S.]]
[[Category: Sun, Z.Y.J.]]
[[Category: Sun, Z Y.J.]]
[[Category: Wagner, G.]]
[[Category: Wagner, G.]]
[[Category: heat repeat-like]]
[[Category: heat repeat-like]]
[[Category: ledgf]]
[[Category: ledgf]]


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