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CRYSTAL STRUCTURE OF THE TOP DOMAIN OF AFRICAN HORSE SICKNESS VIRUS VP7

OverviewOverview

The baculovirus-expressed core protein VP7 of African horse sickness virus serotype 4 (AHSV-4) has been purified to homogeneity and crystallized in the presence of 2.8 M urea. The X-ray structure has been solved to a 2.3-Angstroms (1 Angstrom = 0.1 nm) resolution with an Rfactor of 19.8%. The structure of AHSV VP7 reveals that during crystallization, the two-domain protein is cleaved and only the top domain remains. A similar problem was encountered previously with bluetongue virus (BTV) VP7 (whose structure has been reported), showing that the connections between the top and the bottom domains are rather weak for these two distinct orbiviruses. The top domains of both BTV and AHSV VP7 are trimeric and structurally very similar. The electron density maps show that they both possess an extra electron density feature along their molecular threefold axes, which is most likely due to an unidentified ion. The characteristics of the molecular surface of BTV and AHSV VP7 suggest why AHSV VP7 is much less soluble than BTV VP7 and indicate the possibility of attachment to the cell via attachment of an Arg-Gly-Asp (RGD) motif in the top domain of VP7 to a cellular integrin for both of these orbiviruses.

About this StructureAbout this Structure

1AHS is a Single protein structure of sequence from African horsesickness virus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the top domain of African horse sickness virus VP7: comparisons with bluetongue virus VP7., Basak AK, Gouet P, Grimes J, Roy P, Stuart D, J Virol. 1996 Jun;70(6):3797-806. PMID:8648715

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 '''CRYSTAL STRUCTURE OF THE TOP DOMAIN OF AFRICAN HORSE SICKNESS VIRUS VP7'''<br />
 ==Overview==
-The baculovirus-expressed core protein VP7 of African horse sickness virus, serotype 4 (AHSV-4) has been purified to homogeneity and crystallized in, the presence of 2.8 M urea. The X-ray structure has been solved to a, 2.3-Angstroms (1 Angstrom = 0.1 nm) resolution with an Rfactor of 19.8%., The structure of AHSV VP7 reveals that during crystallization, the, two-domain protein is cleaved and only the top domain remains. A similar, problem was encountered previously with bluetongue virus (BTV) VP7 (whose, structure has been reported), showing that the connections between the top, and the bottom domains are rather weak for these two distinct orbiviruses., The top domains of both BTV and AHSV VP7 are trimeric and structurally, very similar. The electron density maps show that they both possess an, extra electron density feature along their molecular threefold axes, which, is most likely due to an unidentified ion. The characteristics of the, molecular surface of BTV and AHSV VP7 suggest why AHSV VP7 is much less, soluble than BTV VP7 and indicate the possibility of attachment to the, cell via attachment of an Arg-Gly-Asp (RGD) motif in the top domain of VP7, to a cellular integrin for both of these orbiviruses.
+The baculovirus-expressed core protein VP7 of African horse sickness virus serotype 4 (AHSV-4) has been purified to homogeneity and crystallized in the presence of 2.8 M urea. The X-ray structure has been solved to a 2.3-Angstroms (1 Angstrom = 0.1 nm) resolution with an Rfactor of 19.8%. The structure of AHSV VP7 reveals that during crystallization, the two-domain protein is cleaved and only the top domain remains. A similar problem was encountered previously with bluetongue virus (BTV) VP7 (whose structure has been reported), showing that the connections between the top and the bottom domains are rather weak for these two distinct orbiviruses. The top domains of both BTV and AHSV VP7 are trimeric and structurally very similar. The electron density maps show that they both possess an extra electron density feature along their molecular threefold axes, which is most likely due to an unidentified ion. The characteristics of the molecular surface of BTV and AHSV VP7 suggest why AHSV VP7 is much less soluble than BTV VP7 and indicate the possibility of attachment to the cell via attachment of an Arg-Gly-Asp (RGD) motif in the top domain of VP7 to a cellular integrin for both of these orbiviruses.
 ==About this Structure==
-AHS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/African_horsesickness_virus African horsesickness virus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AHS OCA].
+AHS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/African_horsesickness_virus African horsesickness virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AHS OCA].
 ==Reference==
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 [[Category: glycoprotein]]
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