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1qqf

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(New page: 200px<br /><applet load="1qqf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qqf, resolution 1.45&Aring;" /> '''N-TERMINALLY TRUNCAT...)
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[[Image:1qqf.gif|left|200px]]<br /><applet load="1qqf" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1qqf.gif|left|200px]]<br /><applet load="1qqf" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1qqf, resolution 1.45&Aring;" />
caption="1qqf, resolution 1.45&Aring;" />
'''N-TERMINALLY TRUNCATED C3D,G FRAGMENT OF THE COMPLEMENT SYSTEM'''<br />
'''N-TERMINALLY TRUNCATED C3D,G FRAGMENT OF THE COMPLEMENT SYSTEM'''<br />
==Overview==
==Overview==
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Complement component C3 plays a key role in the complement-mediated immune, defence, and occupies a central position within the complement cascade, system. One of its degradation products, C3dg, was purified from rat serum, and crystallised in two different crystal forms as N-terminally truncated, fragment. Despite the truncation and the lack of a significant portion of, the N-terminus as compared to C3d, the structure of the fragment is highly, similar to that of recombinant human C3d (Nagar et al., Science 280 (1998), 1277-1281). Structural details of the reactive site have been obtained, suggesting a possible mode of thioester bond formation between Cys-1010, and Gln-1013 and thioester bond cleavage in the transacylation reaction, involving His-1126. The truncation at the N-terminus of C3d leads to the, exposure of a surface of the molecule that favours dimerisation, so that, in both crystal forms, the fragment is present as a dimer, with monomers, related by a two-fold axis.
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Complement component C3 plays a key role in the complement-mediated immune defence, and occupies a central position within the complement cascade system. One of its degradation products, C3dg, was purified from rat serum and crystallised in two different crystal forms as N-terminally truncated fragment. Despite the truncation and the lack of a significant portion of the N-terminus as compared to C3d, the structure of the fragment is highly similar to that of recombinant human C3d (Nagar et al., Science 280 (1998) 1277-1281). Structural details of the reactive site have been obtained, suggesting a possible mode of thioester bond formation between Cys-1010 and Gln-1013 and thioester bond cleavage in the transacylation reaction involving His-1126. The truncation at the N-terminus of C3d leads to the exposure of a surface of the molecule that favours dimerisation, so that in both crystal forms, the fragment is present as a dimer, with monomers related by a two-fold axis.
==About this Structure==
==About this Structure==
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1QQF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QQF OCA].
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1QQF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QQF OCA].
==Reference==
==Reference==
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[[Category: complement]]
[[Category: complement]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:53:36 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:42:32 2008''

Revision as of 12:42, 21 February 2008


1qqf, resolution 1.45Å

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N-TERMINALLY TRUNCATED C3D,G FRAGMENT OF THE COMPLEMENT SYSTEM

Overview

Complement component C3 plays a key role in the complement-mediated immune defence, and occupies a central position within the complement cascade system. One of its degradation products, C3dg, was purified from rat serum and crystallised in two different crystal forms as N-terminally truncated fragment. Despite the truncation and the lack of a significant portion of the N-terminus as compared to C3d, the structure of the fragment is highly similar to that of recombinant human C3d (Nagar et al., Science 280 (1998) 1277-1281). Structural details of the reactive site have been obtained, suggesting a possible mode of thioester bond formation between Cys-1010 and Gln-1013 and thioester bond cleavage in the transacylation reaction involving His-1126. The truncation at the N-terminus of C3d leads to the exposure of a surface of the molecule that favours dimerisation, so that in both crystal forms, the fragment is present as a dimer, with monomers related by a two-fold axis.

About this Structure

1QQF is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Structure at 1.44 A resolution of an N-terminally truncated form of the rat serum complement C3d fragment., Zanotti G, Bassetto A, Battistutta R, Folli C, Arcidiaco P, Stoppini M, Berni R, Biochim Biophys Acta. 2000 May 23;1478(2):232-8. PMID:10825534

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