1fdp

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[[Image:1fdp.gif|left|200px]]
[[Image:1fdp.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1fdp |SIZE=350|CAPTION= <scene name='initialview01'>1fdp</scene>, resolution 2.1&Aring;
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The line below this paragraph, containing "STRUCTURE_1fdp", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=TRA:Catalytic+Triad'>TRA</scene>, <scene name='pdbsite=TRB:Catalytic+Triad'>TRB</scene>, <scene name='pdbsite=TRC:Catalytic+Triad'>TRC</scene> and <scene name='pdbsite=TRD:Catalytic+Triad'>TRD</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1fdp| PDB=1fdp | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fdp OCA], [http://www.ebi.ac.uk/pdbsum/1fdp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fdp RCSB]</span>
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}}
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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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[[Category: Narayana, S V.L.]]
[[Category: Narayana, S V.L.]]
[[Category: Volanakis, J E.]]
[[Category: Volanakis, J E.]]
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[[Category: complement]]
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[[Category: Complement]]
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[[Category: factor d]]
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[[Category: Factor d]]
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[[Category: proenzyme]]
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[[Category: Proenzyme]]
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[[Category: profactor d]]
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[[Category: Profactor d]]
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[[Category: serine protease]]
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[[Category: Serine protease]]
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[[Category: zymogen]]
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[[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 Sun Mar 30 20:20:54 2008''
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Revision as of 13:12, 2 May 2008

Image:1fdp.gif

Template:STRUCTURE 1fdp

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 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.

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 Page seeded by OCA on Fri May 2 16:12:30 2008

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