3o8e: Difference between revisions
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< | ==Structure of extracelllar portion of CD46 in complex with Adenovirus type 11 knob== | ||
<StructureSection load='3o8e' size='340' side='right'caption='[[3o8e]], [[Resolution|resolution]] 2.84Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3o8e]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_adenovirus_11 Human adenovirus 11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O8E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O8E FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.84Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTD:DITHIANE+DIOL'>DTD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3o8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o8e OCA], [https://pdbe.org/3o8e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o8e RCSB], [https://www.ebi.ac.uk/pdbsum/3o8e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o8e ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q772X2_9ADEN Q772X2_9ADEN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The human membrane cofactor protein (MCP, CD46) is a central component of the innate immune system. CD46 protects autologous cells from complement attack by binding to complement proteins C3b and C4b and serving as a cofactor for their cleavage. Recent data show that CD46 also plays a role in mediating acquired immune responses, and in triggering autophagy. In addition to these physiologic functions, a significant number of pathogens, including select adenoviruses, measles virus, human herpes virus 6 (HHV-6), Streptococci, and Neisseria, use CD46 as a cell attachment receptor. We have determined the crystal structure of the extracellular region of CD46 in complex with the human adenovirus type 11 fiber knob. Extracellular CD46 comprises four short consensus repeats (SCR1-SCR4) that form an elongated structure resembling a hockey stick, with a long shaft and a short blade. Domains SCR1, SCR2 and SCR3 are arranged in a nearly linear fashion. Unexpectedly, however, the structure reveals a profound bend between domains SCR3 and SCR4, which has implications for the interactions with ligands as well as the orientation of the protein at the cell surface. This bend can be attributed to an insertion of five hydrophobic residues in a SCR3 surface loop. Residues in this loop have been implicated in interactions with complement, indicating that the bend participates in binding to C3b and C4b. The structure provides an accurate framework for mapping all known ligand binding sites onto the surface of CD46, thereby advancing an understanding of how CD46 acts as a receptor for pathogens and physiologic ligands of the immune system. | |||
Structure of the extracellular portion of CD46 provides insights into its interactions with complement proteins and pathogens.,Persson BD, Schmitz NB, Santiago C, Zocher G, Larvie M, Scheu U, Casasnovas JM, Stehle T PLoS Pathog. 2010 Sep 30;6(9). pii: e1001122. PMID:20941397<ref>PMID:20941397</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3o8e" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
== | |||
< | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Human adenovirus 11]] | [[Category: Human adenovirus 11]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Casasnovas JM]] | ||
[[Category: | [[Category: Persson BD]] | ||
[[Category: | [[Category: Schmitz NB]] | ||
[[Category: | [[Category: Stehle T]] | ||
Latest revision as of 12:30, 6 September 2023
Structure of extracelllar portion of CD46 in complex with Adenovirus type 11 knobStructure of extracelllar portion of CD46 in complex with Adenovirus type 11 knob
Structural highlights
FunctionPublication Abstract from PubMedThe human membrane cofactor protein (MCP, CD46) is a central component of the innate immune system. CD46 protects autologous cells from complement attack by binding to complement proteins C3b and C4b and serving as a cofactor for their cleavage. Recent data show that CD46 also plays a role in mediating acquired immune responses, and in triggering autophagy. In addition to these physiologic functions, a significant number of pathogens, including select adenoviruses, measles virus, human herpes virus 6 (HHV-6), Streptococci, and Neisseria, use CD46 as a cell attachment receptor. We have determined the crystal structure of the extracellular region of CD46 in complex with the human adenovirus type 11 fiber knob. Extracellular CD46 comprises four short consensus repeats (SCR1-SCR4) that form an elongated structure resembling a hockey stick, with a long shaft and a short blade. Domains SCR1, SCR2 and SCR3 are arranged in a nearly linear fashion. Unexpectedly, however, the structure reveals a profound bend between domains SCR3 and SCR4, which has implications for the interactions with ligands as well as the orientation of the protein at the cell surface. This bend can be attributed to an insertion of five hydrophobic residues in a SCR3 surface loop. Residues in this loop have been implicated in interactions with complement, indicating that the bend participates in binding to C3b and C4b. The structure provides an accurate framework for mapping all known ligand binding sites onto the surface of CD46, thereby advancing an understanding of how CD46 acts as a receptor for pathogens and physiologic ligands of the immune system. Structure of the extracellular portion of CD46 provides insights into its interactions with complement proteins and pathogens.,Persson BD, Schmitz NB, Santiago C, Zocher G, Larvie M, Scheu U, Casasnovas JM, Stehle T PLoS Pathog. 2010 Sep 30;6(9). pii: e1001122. PMID:20941397[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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