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1z9e

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[[Image:1z9e.gif|left|200px]]<br />
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[[Image:1z9e.gif|left|200px]]<br /><applet load="1z9e" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1z9e" size="450" color="white" frame="true" align="right" spinBox="true"
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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==
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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.
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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==
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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].
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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.]]
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[[Category: Sun, Z.Y.J.]]
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[[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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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:31:26 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:13:25 2008''

Revision as of 14:13, 21 February 2008


1z9e

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Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75

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.

About this Structure

1Z9E is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75., Cherepanov P, Sun ZY, Rahman S, Maertens G, Wagner G, Engelman A, Nat Struct Mol Biol. 2005 Jun;12(6):526-32. Epub 2005 May 15. PMID:15895093

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