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Review
. 2008 Aug;82(15):7252-63.
doi: 10.1128/JVI.00104-08. Epub 2008 Apr 2.

Intrinsic structural disorder in adenovirus E1A: a viral molecular hub linking multiple diverse processes

Peter Pelka  1 , Jailal N G Ablack, Gregory J Fonseca, Ahmed F Yousef, Joe S Mymryk
Affiliations
Review

Intrinsic structural disorder in adenovirus E1A: a viral molecular hub linking multiple diverse processes

Peter Pelka et al. J Virol. 2008 Aug.
No abstract available

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Figures

FIG. 1.
FIG. 1.
Map of E1A, CRs, and location of selected MoRFs. The primary HAdV-5 E1A RNA transcript is alternatively spliced to yield two major mRNA-encoding proteins of 289 and 243 residues (R). Comparative analysis of the sequences of the E1A proteins from different HAdV serotypes identified regions of conservation (CR1 to CR4), which are indicated by the colored areas. Selected short linear protein interaction motifs/MoRFs that have been identified within E1A are shown. The E1A sequence and the sequences of other viral and cellular proteins that also use this MoRF for interaction with the target protein are also indicated. Sequence shading indicates residues associated with the consensus of the indicated MoRF (see text for specific details). SMRT, silencing mediator of retinoic acid and thyroid hormone receptor; EBV, Epstein-Barr virus; SV40, simian virus 40; CtIP, CtBP-interacting protein; BRM, Brahma; BKLF, basic Kruppel-like factor.
FIG. 2.
FIG. 2.
Alignment of selected HAdV E1A proteins and prediction of intrinsic disorder. The amino acid sequences of the largest E1A proteins of HAdV-3, -4, -5, -9, -12, and -40, which represent each of the six HAdV subgroups, are shaded with respect to their predicted preference to form intrinsically unstructured regions (black) or structured domains (unshaded). The CRs (CR1 to CR4) are indicated, and sequences are aligned based on amino acid similarity.
FIG. 3.
FIG. 3.
Helical wheel representation of a portion of the N terminus of HAdV-5 E1A. The sequence of HAdV-5 E1A from residues 16 to 28 may form an amphipathic α-helix. (A) Helix viewed from the side. (B) View of helix rotated 180° along the long axis from the view shown in panel A. (C) Top view of helix from the N-terminal end. Nonpolar amino acids are shown in blue, and polar and acidic residues are shown in red.
FIG. 4.
FIG. 4.
The current model of E1A CR3-dependent activation of transcription. Top, linear representation of 289R E1A. CRs are labeled, and AR1 is denoted in yellow. Bottom, residues of E1A CR3 from 139 to 200 are indicated using a one-letter code. The coordinating cysteines are circled, and the key targets of CR3 are shown in green, blue, and red, respectively. The key residues interacting with each target are indicated by the corresponding colors. The boundaries of the residues of CR3 known to be required for interaction with APIS (residues 169 to 188) and the 20S proteasome (residues 161 to 177) are marked by # and *, respectively.
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