1uxb: Difference between revisions
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==Overview== | ==Overview== | ||
Adenovirus serotype 37 (Ad37) belongs to species D and can cause epidemic, keratoconjunctivitis, whereas the closely related Ad19p does not. Primary, cell attachment by adenoviruses is mediated through receptor binding of, the knob domain of the fiber protein. The knobs of Ad37 and Ad19p differ, at only two positions, Lys240Glu and Asn340Asp. We report the, high-resolution crystal structures of the Ad37 and Ad19p knobs, both, native and in complex with sialic acid, which has been proposed as a, receptor for Ad37. Overall, the Ad37 and Ad19p knobs are very similar to, previously reported knob structures, especially to that of Ad5, which, binds the coxsackievirus-adenovirus receptor (CAR). Ad37 and Ad19p knobs, are structurally identical with the exception of the changed side chains, and ... | Adenovirus serotype 37 (Ad37) belongs to species D and can cause epidemic, keratoconjunctivitis, whereas the closely related Ad19p does not. Primary, cell attachment by adenoviruses is mediated through receptor binding of, the knob domain of the fiber protein. The knobs of Ad37 and Ad19p differ, at only two positions, Lys240Glu and Asn340Asp. We report the, high-resolution crystal structures of the Ad37 and Ad19p knobs, both, native and in complex with sialic acid, which has been proposed as a, receptor for Ad37. Overall, the Ad37 and Ad19p knobs are very similar to, previously reported knob structures, especially to that of Ad5, which, binds the coxsackievirus-adenovirus receptor (CAR). Ad37 and Ad19p knobs, are structurally identical with the exception of the changed side chains, and are structurally most similar to CAR-binding knobs (e.g., that of Ad5), rather than non-CAR-binding knobs (e.g., that of Ad3). The two mutations, in Ad19p result in a partial loss of the exceptionally high positive, surface charge of the Ad37 knob but do not affect sialic acid binding., This site is located on the top of the trimer and binds both alpha(2,3), and alpha(2,6)-linked sialyl-lactose, although only the sialic acid, residue makes direct contact. Amino acid alignment suggests that the, sialic acid binding site is conserved in several species D serotypes. Our, results show that the altered viral tropism and cell binding of Ad19p, relative to those of Ad37 are not explained by a different binding ability, toward sialyl-lactose. | ||
==About this Structure== | ==About this Structure== | ||
1UXB is a | 1UXB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_adenovirus_type_15 Human adenovirus type 15] with ZN and ACT as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UXB OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: sialic acid]] | [[Category: sialic acid]] | ||
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Revision as of 15:27, 5 November 2007
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ADENOVIRUS AD19P FIBRE HEAD IN COMPLEX WITH SIALYL-LACTOSE
OverviewOverview
Adenovirus serotype 37 (Ad37) belongs to species D and can cause epidemic, keratoconjunctivitis, whereas the closely related Ad19p does not. Primary, cell attachment by adenoviruses is mediated through receptor binding of, the knob domain of the fiber protein. The knobs of Ad37 and Ad19p differ, at only two positions, Lys240Glu and Asn340Asp. We report the, high-resolution crystal structures of the Ad37 and Ad19p knobs, both, native and in complex with sialic acid, which has been proposed as a, receptor for Ad37. Overall, the Ad37 and Ad19p knobs are very similar to, previously reported knob structures, especially to that of Ad5, which, binds the coxsackievirus-adenovirus receptor (CAR). Ad37 and Ad19p knobs, are structurally identical with the exception of the changed side chains, and are structurally most similar to CAR-binding knobs (e.g., that of Ad5), rather than non-CAR-binding knobs (e.g., that of Ad3). The two mutations, in Ad19p result in a partial loss of the exceptionally high positive, surface charge of the Ad37 knob but do not affect sialic acid binding., This site is located on the top of the trimer and binds both alpha(2,3), and alpha(2,6)-linked sialyl-lactose, although only the sialic acid, residue makes direct contact. Amino acid alignment suggests that the, sialic acid binding site is conserved in several species D serotypes. Our, results show that the altered viral tropism and cell binding of Ad19p, relative to those of Ad37 are not explained by a different binding ability, toward sialyl-lactose.
About this StructureAbout this Structure
1UXB is a Single protein structure of sequence from Human adenovirus type 15 with ZN and ACT as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of species D adenovirus fiber knobs and their sialic acid binding sites., Burmeister WP, Guilligay D, Cusack S, Wadell G, Arnberg N, J Virol. 2004 Jul;78(14):7727-36. PMID:15220447
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