2i6q

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[[Image:2i6q.gif|left|200px]]<br /><applet load="2i6q" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2i6q.gif|left|200px]]
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caption="2i6q, resolution 2.100&Aring;" />
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'''Complement component C2a'''<br />
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{{Structure
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|PDB= 2i6q |SIZE=350|CAPTION= <scene name='initialview01'>2i6q</scene>, resolution 2.100&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=MLI:MALONATE ION'>MLI</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Classical-complement-pathway_C3/C5_convertase Classical-complement-pathway C3/C5 convertase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.43 3.4.21.43]
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|GENE= C2a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Complement component C2a'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2I6Q 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=NAG:'>NAG</scene>, <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=MLI:'>MLI</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Classical-complement-pathway_C3/C5_convertase Classical-complement-pathway C3/C5 convertase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.43 3.4.21.43] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I6Q OCA].
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2I6Q 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=2I6Q OCA].
==Reference==
==Reference==
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Structure of complement component C2A: implications for convertase formation and substrate binding., Milder FJ, Raaijmakers HC, Vandeputte MD, Schouten A, Huizinga EG, Romijn RA, Hemrika W, Roos A, Daha MR, Gros P, Structure. 2006 Oct;14(10):1587-97. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17027507 17027507]
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Structure of complement component C2A: implications for convertase formation and substrate binding., Milder FJ, Raaijmakers HC, Vandeputte MD, Schouten A, Huizinga EG, Romijn RA, Hemrika W, Roos A, Daha MR, Gros P, Structure. 2006 Oct;14(10):1587-97. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17027507 17027507]
[[Category: Classical-complement-pathway C3/C5 convertase]]
[[Category: Classical-complement-pathway C3/C5 convertase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: von willebrand factor-a domain]]
[[Category: von willebrand factor-a domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:49:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:26:06 2008''

Revision as of 15:26, 20 March 2008


PDB ID 2i6q

Drag the structure with the mouse to rotate
, resolution 2.100Å
Ligands: , and
Gene: C2a (Homo sapiens)
Activity: Classical-complement-pathway C3/C5 convertase, with EC number 3.4.21.43
Coordinates: save as pdb, mmCIF, xml



Complement component C2a


Contents

Overview

C2a provides the catalytic center to the convertase complexes of the classical and lectin-binding pathways of complement activation. We determined two crystal structures of full-length C2a, with and without a pseudo ligand bound. Both structures reveal a near-active conformation of the catalytic center of the serine protease domains, while the von Willebrand factor A-type domains display an intermediate activation state of helix alpha7 with an open, activated metal-ion-dependent adhesion site. The open adhesion site likely serves to enhance the affinity for the ligand C4b, similar to "inside-out" signaling in integrins. Surprisingly, the N-terminal residues of C2a are buried in a crevice near helix alpha7, indicative of a structural switch between C2 and C2a. Extended loops on the protease domain possibly envelop the protruding anaphylatoxin domain of the substrate C3. Together with a putative substrate-induced completion of the oxyanion hole, this may contribute to the high substrate specificity of the convertases.

Disease

Known diseases associated with this structure: C2 deficiency OMIM:[217000], Macular degeneration, age-related, reduced risk of OMIM:[217000]

About this Structure

2I6Q is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of complement component C2A: implications for convertase formation and substrate binding., Milder FJ, Raaijmakers HC, Vandeputte MD, Schouten A, Huizinga EG, Romijn RA, Hemrika W, Roos A, Daha MR, Gros P, Structure. 2006 Oct;14(10):1587-97. PMID:17027507

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