2jg9
From Proteopedia
Line 1: | Line 1: | ||
[[Image:2jg9.jpg|left|200px]] | [[Image:2jg9.jpg|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_2jg9", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | + | --> | |
- | + | {{STRUCTURE_2jg9| PDB=2jg9 | SCENE= }} | |
- | + | ||
- | + | ||
- | }} | + | |
'''CRYSTALLOGRAPHIC STRUCTURE OF HUMAN C1Q GLOBULAR HEADS (P1)''' | '''CRYSTALLOGRAPHIC STRUCTURE OF HUMAN C1Q GLOBULAR HEADS (P1)''' | ||
Line 33: | Line 30: | ||
[[Category: Paidassi, H.]] | [[Category: Paidassi, H.]] | ||
[[Category: Tacnet-Delorme, P.]] | [[Category: Tacnet-Delorme, P.]] | ||
- | [[Category: | + | [[Category: Apopotosis]] |
- | [[Category: | + | [[Category: Cell surface molecule]] |
- | [[Category: | + | [[Category: Collagen]] |
- | [[Category: | + | [[Category: Complement]] |
- | [[Category: | + | [[Category: Complement pathway]] |
- | [[Category: | + | [[Category: Disease mutation]] |
- | [[Category: | + | [[Category: Glycoprotein]] |
- | [[Category: | + | [[Category: Hydroxylation]] |
- | [[Category: | + | [[Category: Immune response]] |
- | [[Category: | + | [[Category: Immune system]] |
- | [[Category: | + | [[Category: Innate immunity]] |
- | [[Category: | + | [[Category: Phagocytosis]] |
- | [[Category: | + | [[Category: Polymorphism]] |
- | [[Category: | + | [[Category: Pyrrolidone carboxylic acid]] |
- | [[Category: | + | [[Category: Tolerance]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:51:50 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 05:51, 4 May 2008
CRYSTALLOGRAPHIC STRUCTURE OF HUMAN C1Q GLOBULAR HEADS (P1)
Overview
Efficient apoptotic cell clearance is critical for maintenance of tissue homeostasis, and to control the immune responses mediated by phagocytes. Little is known about the molecules that contribute "eat me" signals on the apoptotic cell surface. C1q, the recognition unit of the C1 complex of complement, also senses altered structures from self and is a major actor of immune tolerance. HeLa cells were rendered apoptotic by UV-B treatment and a variety of cellular and molecular approaches were used to investigate the nature of the target(s) recognized by C1q. Using surface plasmon resonance, C1q binding was shown to occur at early stages of apoptosis and to involve recognition of a cell membrane component. C1q binding and phosphatidylserine (PS) exposure, as measured by annexin V labeling, proceeded concomitantly, and annexin V inhibited C1q binding in a dose-dependent manner. As shown by cosedimentation, surface plasmon resonance, and x-ray crystallographic analyses, C1q recognized PS specifically and avidly (K(D) = 3.7-7 x 10(-8) M), through multiple interactions between its globular domain and the phosphoserine group of PS. Confocal microscopy revealed that the majority of the C1q molecules were distributed in membrane patches where they colocalized with PS. In summary, PS is one of the C1q ligands on apoptotic cells, and C1q-PS interaction takes place at early stages of apoptosis, in newly organized membrane patches. Given its versatile recognition properties, these data suggest that C1q has the unique ability to sense different markers which collectively would provide strong eat me signals, thereby allowing efficient apoptotic cell removal.
About this Structure
2JG9 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
C1q Binds Phosphatidylserine and Likely Acts as a Multiligand-Bridging Molecule in Apoptotic Cell Recognition., Paidassi H, Tacnet-Delorme P, Garlatti V, Darnault C, Ghebrehiwet B, Gaboriaud C, Arlaud GJ, Frachet P, J Immunol. 2008 Feb 15;180(4):2329-2338. PMID:18250442 Page seeded by OCA on Sun May 4 08:51:50 2008
Categories: Homo sapiens | Protein complex | Arlaud, G J. | Darnault, C. | Frachet, P. | Gaboriaud, C. | Garlatti, V. | Ghebrehiwet, B. | Paidassi, H. | Tacnet-Delorme, P. | Apopotosis | Cell surface molecule | Collagen | Complement | Complement pathway | Disease mutation | Glycoprotein | Hydroxylation | Immune response | Immune system | Innate immunity | Phagocytosis | Polymorphism | Pyrrolidone carboxylic acid | Tolerance