id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-299848-fft1brwz	Claridge, Jolyon K.	A picornaviral loop-to-loop replication complex	2009-03-04		.txt	text/plain	8818	459	60	Using human rhinovirus as a model system, we have combined NMR contact information, small-angle X-ray scattering (SAXS) data, and previous mutagenesis results to determine the shape, position and relative orientation of the 3C(pro) and SLD components. Binding between SLD and 3C(pro) induces structural changes in the proteolytic active site that is positioned on the opposite side of the protease relative to the RNA/protein interface, suggesting that subtle conformational changes affecting catalytic activity are relayed through the protein. NMR and small-angle X-ray scattering data were combined with results from previous mutational analysis (Andino et al., 1993; Leong et al., 1993) (Fig. 1) to construct a structural model of the HRV-14 3C pro -SLD complex. The largest SLD-induced chemical shift perturbations on the 3C pro surface cluster primarily to a patch (dark red in Fig. 5A ) that includes D32 from the loop connecting b-strands 2-3, N80, F83 and F89 from the inter-domain linker and V179 from the C-terminal region.	./cache/cord-299848-fft1brwz.txt	./txt/cord-299848-fft1brwz.txt