1hfd
From Proteopedia
(New page: 200px<br /> <applet load="1hfd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hfd, resolution 2.3Å" /> '''HUMAN COMPLEMENT FAC...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1HFD is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.46 3.4.21.46]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HFD OCA]]. | + | 1HFD is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]]. Active as [[http://en.wikipedia.org/wiki/Complement_factor_D Complement factor D]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.46 3.4.21.46]]. Structure known Active Site: NUL. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HFD OCA]]. |
==Reference== | ==Reference== | ||
Structures of native and complexed complement factor D: implications of the atypical His57 conformation and self-inhibitory loop in the regulation of specific serine protease activity., Jing H, Babu YS, Moore D, Kilpatrick JM, Liu XY, Volanakis JE, Narayana SV, J Mol Biol. 1998 Oct 9;282(5):1061-81. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9753554 9753554] | Structures of native and complexed complement factor D: implications of the atypical His57 conformation and self-inhibitory loop in the regulation of specific serine protease activity., Jing H, Babu YS, Moore D, Kilpatrick JM, Liu XY, Volanakis JE, Narayana SV, J Mol Biol. 1998 Oct 9;282(5):1061-81. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9753554 9753554] | ||
| + | [[Category: Complement factor D]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: serine protease]] | [[Category: serine protease]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:49:13 2007'' |
Revision as of 11:44, 30 October 2007
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HUMAN COMPLEMENT FACTOR D IN A P21 CRYSTAL FORM
Overview
Factor D is a serine protease essential for the activation of the, alternative pathway of complement. The structures of native factor D and a, complex formed with isatoic anhydride inhibitor were determined at, resolution of 2.3 and 1.5 A, respectively, in an isomorphous monoclinic, crystal form containing one molecule per asymmetric unit. The native, structure was compared with structures determined previously in a, triclinic cell containing two molecules with different active site, conformations. The current structure shows greater similarity with, molecule B in the triclinic cell, suggesting that this may be the dominant, factor D conformation in solution. The major conformational differences, with molecule A in the triclinic cell are located in four regions, three, of which are close ... [(full description)]
About this Structure
1HFD is a [Single protein] structure of sequence from [Homo sapiens]. Active as [Complement factor D], with EC number [3.4.21.46]. Structure known Active Site: NUL. Full crystallographic information is available from [OCA].
Reference
Structures of native and complexed complement factor D: implications of the atypical His57 conformation and self-inhibitory loop in the regulation of specific serine protease activity., Jing H, Babu YS, Moore D, Kilpatrick JM, Liu XY, Volanakis JE, Narayana SV, J Mol Biol. 1998 Oct 9;282(5):1061-81. PMID:9753554
Page seeded by OCA on Tue Oct 30 13:49:13 2007
