1fdp
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(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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Revision as of 18:07, 29 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 [[1]], with EC number [3.4.21.46]. 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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