1e0e
From Proteopedia
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|PDB= 1e0e |SIZE=350|CAPTION= <scene name='initialview01'>1e0e</scene> | |PDB= 1e0e |SIZE=350|CAPTION= <scene name='initialview01'>1e0e</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e0e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e0e OCA], [http://www.ebi.ac.uk/pdbsum/1e0e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e0e RCSB]</span> | ||
}} | }} | ||
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[[Category: Kaptein, R.]] | [[Category: Kaptein, R.]] | ||
[[Category: Plasterk, R H.A.]] | [[Category: Plasterk, R H.A.]] | ||
| - | [[Category: ZN]] | ||
[[Category: aid]] | [[Category: aid]] | ||
[[Category: dimer]] | [[Category: dimer]] | ||
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[[Category: zinc-binding protein]] | [[Category: zinc-binding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:52:25 2008'' |
Revision as of 16:52, 30 March 2008
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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