1dsu: Difference between revisions
New page: left|200px<br /> <applet load="1dsu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dsu, resolution 2.0Å" /> '''HUMAN FACTOR D, COMP... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1dsu.gif|left|200px]]<br /> | [[Image:1dsu.gif|left|200px]]<br /><applet load="1dsu" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1dsu" size=" | |||
caption="1dsu, resolution 2.0Å" /> | caption="1dsu, resolution 2.0Å" /> | ||
'''HUMAN FACTOR D, COMPLEMENT ACTIVATING ENZYME'''<br /> | '''HUMAN FACTOR D, COMPLEMENT ACTIVATING ENZYME'''<br /> | ||
==Overview== | ==Overview== | ||
Factor D, an essential enzyme for the activation of the alternative | Factor D, an essential enzyme for the activation of the alternative pathway of the complement system, belongs to the serine protease superfamily. The crystal structure of the enzyme was solved by a combination of multiple isomorphous replacement and molecular replacement methods. The present model was refined to an R-factor of 18.8% using 23,681 observed reflections between 7.5 and 2.0 A resolution, with a root-mean-square deviation from standard bond lengths of 0.016 A. The two non-crystallographically related molecules in the triclinic unit cell have distinctive active site conformations. The protein has the general structural fold of a serine protease, but there are several unique amino acid substitutions resulting in significant alterations in the critical loops responsible for catalysis and substrate specificity in serine proteases. Factor D is the first complement serine protease whose three-dimensional structure has been determined. | ||
==Disease== | ==Disease== | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
1DSU 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] Full crystallographic information is available from [http:// | 1DSU 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DSU OCA]. | ||
==Reference== | ==Reference== | ||
| Line 18: | Line 17: | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Delucas, L | [[Category: Delucas, L J.]] | ||
[[Category: Narayana, S | [[Category: Narayana, S V.L.]] | ||
[[Category: Volanakis, J | [[Category: Volanakis, J E.]] | ||
[[Category: complement activating enzyme]] | [[Category: complement activating enzyme]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: serine protease]] | [[Category: serine protease]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:05 2008'' | ||
Revision as of 13:20, 21 February 2008
|
HUMAN FACTOR D, COMPLEMENT ACTIVATING ENZYME
OverviewOverview
Factor D, an essential enzyme for the activation of the alternative pathway of the complement system, belongs to the serine protease superfamily. The crystal structure of the enzyme was solved by a combination of multiple isomorphous replacement and molecular replacement methods. The present model was refined to an R-factor of 18.8% using 23,681 observed reflections between 7.5 and 2.0 A resolution, with a root-mean-square deviation from standard bond lengths of 0.016 A. The two non-crystallographically related molecules in the triclinic unit cell have distinctive active site conformations. The protein has the general structural fold of a serine protease, but there are several unique amino acid substitutions resulting in significant alterations in the critical loops responsible for catalysis and substrate specificity in serine proteases. Factor D is the first complement serine protease whose three-dimensional structure has been determined.
DiseaseDisease
Known diseases associated with this structure: Azoospermia OMIM:[400005], Complement factor D deficiency OMIM:[134350], Corneal fleck dystrophy OMIM:[609414], Properdin deficiency, X-linked OMIM:[300383]
About this StructureAbout this Structure
1DSU is a Single protein structure of sequence from Homo sapiens. Active as Complement factor D, with EC number 3.4.21.46 Full crystallographic information is available from OCA.
ReferenceReference
Structure of human factor D. A complement system protein at 2.0 A resolution., Narayana SV, Carson M, el-Kabbani O, Kilpatrick JM, Moore D, Chen X, Bugg CE, Volanakis JE, DeLucas LJ, J Mol Biol. 1994 Jan 14;235(2):695-708. PMID:8289289
Page seeded by OCA on Thu Feb 21 12:20:05 2008