1e0e

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(New page: 200px<br /> <applet load="1e0e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e0e" /> '''N-TERMINAL ZINC-BINDING HHCC DOMAIN OF HIV-...)
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'''N-TERMINAL ZINC-BINDING HHCC DOMAIN OF HIV-2 INTEGRASE'''<br />
'''N-TERMINAL ZINC-BINDING HHCC DOMAIN OF HIV-2 INTEGRASE'''<br />
==Overview==
==Overview==
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The solution structure of the dimeric N-terminal domain of HIV-2 integrase, (residues 1-55, named IN(1-55)) has been determined using NMR, spectroscopy. The structure of the monomer, which was already reported, previously [Eijkelenboom et al. (1997) Curr. Biol., 7, 739-746], consists, of four alpha-helices and is well defined. Helices alpha1, alpha2 and, alpha3 form a three-helix bundle that is stabilized by zinc binding to, His12, His16, Cys40 and Cys43. The dimer interface is formed by the, N-terminal tail and the first half of helix alpha3. The orientation of the, two monomeric units with respect to each other shows considerable, variation. 15N relaxation studies have been used to characterize the, nature of the intermonomeric disorder. Comparison of the dimer interface, with that of the well-defined dimer interface of HIV-1 IN(1-55) shows that, the latter is stabilized by additional hydrophobic interactions and a, potential salt bridge. Similar interactions cannot be formed in HIV-2, IN(1-55) [Cai et al. (1997) Nat. Struct. Biol., 4, 567-577], where the, corresponding residues are positively charged and neutral ones.
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The solution structure of the dimeric N-terminal domain of HIV-2 integrase (residues 1-55, named IN(1-55)) has been determined using NMR spectroscopy. The structure of the monomer, which was already reported previously [Eijkelenboom et al. (1997) Curr. Biol., 7, 739-746], consists of four alpha-helices and is well defined. Helices alpha1, alpha2 and alpha3 form a three-helix bundle that is stabilized by zinc binding to His12, His16, Cys40 and Cys43. The dimer interface is formed by the N-terminal tail and the first half of helix alpha3. The orientation of the two monomeric units with respect to each other shows considerable variation. 15N relaxation studies have been used to characterize the nature of the intermonomeric disorder. Comparison of the dimer interface with that of the well-defined dimer interface of HIV-1 IN(1-55) shows that the latter is stabilized by additional hydrophobic interactions and a potential salt bridge. Similar interactions cannot be formed in HIV-2 IN(1-55) [Cai et al. (1997) Nat. Struct. Biol., 4, 567-577], where the corresponding residues are positively charged and neutral ones.
==About this Structure==
==About this Structure==
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1E0E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Viruses Viruses] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 1AUB. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E0E OCA].
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1E0E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Viruses Viruses] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1AUB. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E0E OCA].
==Reference==
==Reference==
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[[Category: Viruses]]
[[Category: Viruses]]
[[Category: Boelens, R.]]
[[Category: Boelens, R.]]
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[[Category: Eijkelenboom, A.P.A.M.]]
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[[Category: Eijkelenboom, A P.A M.]]
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[[Category: Ent, F.M.I.Van.Den.]]
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[[Category: Ent, F M.I Van Den.]]
[[Category: Kaptein, R.]]
[[Category: Kaptein, R.]]
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[[Category: Plasterk, R.H.A.]]
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[[Category: Plasterk, R H.A.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: aids]]
[[Category: aids]]
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[[Category: zinc-binding protein]]
[[Category: zinc-binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 13:59:31 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:22:26 2008''

Revision as of 10:22, 21 February 2008


1e0e

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N-TERMINAL ZINC-BINDING HHCC DOMAIN OF HIV-2 INTEGRASE

Overview

The solution structure of the dimeric N-terminal domain of HIV-2 integrase (residues 1-55, named IN(1-55)) has been determined using NMR spectroscopy. The structure of the monomer, which was already reported previously [Eijkelenboom et al. (1997) Curr. Biol., 7, 739-746], consists of four alpha-helices and is well defined. Helices alpha1, alpha2 and alpha3 form a three-helix bundle that is stabilized by zinc binding to His12, His16, Cys40 and Cys43. The dimer interface is formed by the N-terminal tail and the first half of helix alpha3. The orientation of the two monomeric units with respect to each other shows considerable variation. 15N relaxation studies have been used to characterize the nature of the intermonomeric disorder. Comparison of the dimer interface with that of the well-defined dimer interface of HIV-1 IN(1-55) shows that the latter is stabilized by additional hydrophobic interactions and a potential salt bridge. Similar interactions cannot be formed in HIV-2 IN(1-55) [Cai et al. (1997) Nat. Struct. Biol., 4, 567-577], where the corresponding residues are positively charged and neutral ones.

About this Structure

1E0E is a Single protein structure of sequence from Viruses with as ligand. This structure supersedes the now removed PDB entry 1AUB. Full crystallographic information is available from OCA.

Reference

Refined solution structure of the dimeric N-terminal HHCC domain of HIV-2 integrase., Eijkelenboom AP, van den Ent FM, Wechselberger R, Plasterk RH, Kaptein R, Boelens R, J Biomol NMR. 2000 Oct;18(2):119-28. PMID:11101216

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