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| {{STRUCTURE_1fdp| PDB=1fdp | SCENE= }} | | {{STRUCTURE_1fdp| PDB=1fdp | SCENE= }} |
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| '''PROENZYME OF HUMAN COMPLEMENT FACTOR D, RECOMBINANT PROFACTOR D'''
| | ===PROENZYME OF HUMAN COMPLEMENT FACTOR D, RECOMBINANT PROFACTOR D=== |
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| ==Overview==
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| 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 initial positioning role for the N-terminus, and Leu17 probably also helps in inducing the required conformational changes. This process, perhaps shared by most chymotrypsinogen-like zymogens, is followed by a factor D-unique step, the re-orientation of an external Arg218 to an internal position for salt-bridging with Asp189, leading to the generation of the self-inhibited factor D. | | The line below this paragraph, {{ABSTRACT_PUBMED_10022823}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10022823 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10022823}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Serine protease]] | | [[Category: Serine protease]] |
| [[Category: Zymogen]] | | [[Category: Zymogen]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:12:30 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:06:14 2008'' |
