1md7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1md7.gif|left|200px]]<br /><applet load="1md7" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1md7.gif|left|200px]]
-
caption="1md7, resolution 3.20&Aring;" />
+
 
-
'''Monomeric structure of the zymogen of complement protease C1r'''<br />
+
{{Structure
 +
|PDB= 1md7 |SIZE=350|CAPTION= <scene name='initialview01'>1md7</scene>, resolution 3.20&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/Complement_subcomponent_C1r Complement subcomponent C1r], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.41 3.4.21.41]
 +
|GENE=
 +
}}
 +
 
 +
'''Monomeric structure of the zymogen of complement protease C1r'''
 +
 
==Overview==
==Overview==
Line 10: Line 19:
==About this Structure==
==About this Structure==
-
1MD7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NDG:'>NDG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Complement_subcomponent_C1r Complement subcomponent C1r], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.41 3.4.21.41] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MD7 OCA].
+
1MD7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MD7 OCA].
==Reference==
==Reference==
-
Monomeric structures of the zymogen and active catalytic domain of complement protease c1r: further insights into the c1 activation mechanism., Budayova-Spano M, Grabarse W, Thielens NM, Hillen H, Lacroix M, Schmidt M, Fontecilla-Camps JC, Arlaud GJ, Gaboriaud C, Structure. 2002 Nov;10(11):1509-19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12429092 12429092]
+
Monomeric structures of the zymogen and active catalytic domain of complement protease c1r: further insights into the c1 activation mechanism., Budayova-Spano M, Grabarse W, Thielens NM, Hillen H, Lacroix M, Schmidt M, Fontecilla-Camps JC, Arlaud GJ, Gaboriaud C, Structure. 2002 Nov;10(11):1509-19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12429092 12429092]
[[Category: Complement subcomponent C1r]]
[[Category: Complement subcomponent C1r]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
Line 33: Line 42:
[[Category: substrate specificity]]
[[Category: substrate specificity]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:54:02 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:42:05 2008''

Revision as of 10:42, 20 March 2008

Image:1md7.gif


PDB ID 1md7

Drag the structure with the mouse to rotate
, resolution 3.20Å
Ligands:
Activity: Complement subcomponent C1r, with EC number 3.4.21.41
Coordinates: save as pdb, mmCIF, xml



Monomeric structure of the zymogen of complement protease C1r


Contents

Overview

C1r is the serine protease (SP) that mediates autoactivation of C1, the complex that triggers the classical complement pathway. We have determined the crystal structure of two fragments from the human C1r catalytic domain, each encompassing the second complement control protein (CCP2) module and the SP domain. The wild-type species has an active structure, whereas the S637A mutant is a zymogen. The structures reveal a restricted hinge flexibility of the CCP2-SP interface, and both are characterized by the unique alpha-helical conformation of loop E. The zymogen activation domain exhibits high mobility, and the active structure shows a restricted access to most substrate binding subsites. Further implications relevant to the C1r self-activation process are derived from protein-protein interactions in the crystals.

Disease

Known disease associated with this structure: C1r/C1s deficiency, combined OMIM:[216950]

About this Structure

1MD7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Monomeric structures of the zymogen and active catalytic domain of complement protease c1r: further insights into the c1 activation mechanism., Budayova-Spano M, Grabarse W, Thielens NM, Hillen H, Lacroix M, Schmidt M, Fontecilla-Camps JC, Arlaud GJ, Gaboriaud C, Structure. 2002 Nov;10(11):1509-19. PMID:12429092

Page seeded by OCA on Thu Mar 20 12:42:05 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1md7"
Personal tools