Figure 6. Schematic of the domain structure of retroviral integrases.

Figure 6

Schematic of the domain structure of retroviral integrases. The three domains appear to be stably folded when prepared separately. The amino-terminal-most (HHCC) domain is characterized by pairs of histidine and cysteine residues that are universally conserved among retroviral integrases. The central domain contains the catalytic site. It is characterized by a triad of universally conserved and essential residues, an aspartate, followed at some distance by an aspartate and glutamic acid that are always separated by 35 amino acids. The three-dimensional structure of this domain has been determined for HIV-1 integrase (Dyda et al. 1994), and for ASV integrase (Bujacz et al. 1995, 1996) (Fig. 7). The carboxy-terminal domain is sometimes called the DNA-binding domain, a bit of a misnomer since the core domain also binds DNA, but nevertheless an accurate reflection of its one known activity. The three-dimensional solution structure of this domain from HIV-1 integrase has been determined by NMR (Eijkelenboom et al. 1995; Lodi et al. 1995).

From: Biochemical Activities and Assays

Cover of Retroviruses
Coffin JM, Hughes SH, Varmus HE, editors.
Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 1997.
Copyright © 1997, Cold Spring Harbor Laboratory Press.

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