1fdp
From Proteopedia
(New page: 200px<br /> <applet load="1fdp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fdp, resolution 2.1Å" /> '''PROENZYME OF HUMAN C...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1FDP 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=1FDP OCA]]. | + | 1FDP 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 Sites: TRA, TRB, TRC and TRD. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FDP OCA]]. |
==Reference== | ==Reference== | ||
Structural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D., Jing H, Macon KJ, Moore D, DeLucas LJ, Volanakis JE, Narayana SV, EMBO J. 1999 Feb 15;18(4):804-14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10022823 10022823] | Structural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D., Jing H, Macon KJ, Moore D, DeLucas LJ, Volanakis JE, Narayana SV, EMBO J. 1999 Feb 15;18(4):804-14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10022823 10022823] | ||
| + | [[Category: Complement factor D]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: zymogen]] | [[Category: zymogen]] | ||
| - | ''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 13:07:38 2007'' |
Revision as of 11:02, 30 October 2007
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PROENZYME OF HUMAN COMPLEMENT FACTOR D, RECOMBINANT PROFACTOR D
Overview
The crystal structure of profactor D, determined at 2.1 A resolution with, an Rfree and an R-factor of 25.1 and 20.4%, respectively, displays highly, flexible or disordered conformation for five regions: N-22, 71-76, 143-152, 187-193 and 215-223. A comparison with the structure of its, mature serine protease, complement factor D, revealed major conformational, changes in the similar regions. Comparisons with the zymogen-active enzyme, pairs of chymotrypsinogen, trypsinogen and prethrombin-2 showed a similar, distribution of the flexible regions. However, profactor D is the most, flexible of the four, and its mature enzyme displays inactive, self-inhibited active site conformation. Examination of the surface, properties of the N-terminus-binding pocket indicates that Ile16 may play, the ... [(full description)]
About this Structure
1FDP 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 Sites: TRA, TRB, TRC and TRD. Full crystallographic information is available from [OCA].
Reference
Structural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D., Jing H, Macon KJ, Moore D, DeLucas LJ, Volanakis JE, Narayana SV, EMBO J. 1999 Feb 15;18(4):804-14. PMID:10022823
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