1fdp

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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'''
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===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.
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(as it appears on PubMed at http://www.pubmed.gov), where 10022823 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10022823}}
==About this Structure==
==About this Structure==
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[[Category: Serine protease]]
[[Category: Serine protease]]
[[Category: Zymogen]]
[[Category: Zymogen]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:12:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:06:14 2008''

Revision as of 00:06, 1 July 2008

Image:1fdp.png

Template:STRUCTURE 1fdp

PROENZYME OF HUMAN COMPLEMENT FACTOR D, RECOMBINANT PROFACTOR D

Template:ABSTRACT PUBMED 10022823

About this Structure

1FDP is a Single protein structure of sequence from Homo sapiens. 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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