Summary for 1E0E
| Entry DOI | 10.2210/pdb1e0e/pdb |
| NMR Information | BMRB: 4619 |
| Descriptor | HUMAN IMMUNODEFICIENCY VIRUS TYPE 2 INTEGRASE, ZINC ION (2 entities in total) |
| Functional Keywords | integrase, aids, polyprotein, dimer, zinc-binding protein, helix-turn-helix motif |
| Biological source | HUMAN IMMUNODEFICIENCY VIRUS TYPE 2 (ISOLATE ROD) (HIV-2) |
| Total number of polymer chains | 2 |
| Total formula weight | 12662.90 |
| Authors | Eijkelenboom, A.P.A.M.,Van Den ent, F.M.I.,Plasterk, R.H.A.,Kaptein, R.,Boelens, R. (deposition date: 2000-03-25, release date: 2001-03-19, Last modification date: 2024-05-15) |
| Primary citation | Eijkelenboom, A.P.A.M.,Van Den Ent, F.M.I.,Wechselberger, R.,Plasterk, R.H.A.,Kaptein, R.,Boelens, R. Refined Solution Structure of the Dimeric N-Terminal Hhcc Domain of HIV-2 Integrase J.Biomol.NMR, 18:119-, 2000 Cited by PubMed Abstract: 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. PubMed: 11101216DOI: 10.1023/A:1008342312269 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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