1pk6: Difference between revisions

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|PDB= 1pk6 |SIZE=350|CAPTION= <scene name='initialview01'>1pk6</scene>, resolution 1.85&Aring;
|PDB= 1pk6 |SIZE=350|CAPTION= <scene name='initialview01'>1pk6</scene>, resolution 1.85&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=[[1gpz|1GPZ]], [[1elv|1ELV]], [[1nzi|1NZI]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pk6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pk6 OCA], [http://www.ebi.ac.uk/pdbsum/1pk6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pk6 RCSB]</span>
}}
}}


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==Overview==
==Overview==
C1q is a versatile recognition protein that binds to an amazing variety of immune and non-immune ligands and triggers activation of the classical pathway of complement. The crystal structure of the C1q globular domain responsible for its recognition properties has now been solved and refined to 1.9 A of resolution. The structure reveals a compact, almost spherical heterotrimeric assembly held together mainly by non-polar interactions, with a Ca2+ ion bound at the top. The heterotrimeric assembly of the C1q globular domain appears to be a key factor of the versatile recognition properties of this protein. Plausible three-dimensional models of the C1q globular domain in complex with two of its physiological ligands, C-reactive protein and IgG, are proposed, highlighting two of the possible recognition modes of C1q. The C1q/human IgG1 model suggests a critical role for the hinge region of IgG and for the relative orientation of its Fab domain in C1q binding.
C1q is a versatile recognition protein that binds to an amazing variety of immune and non-immune ligands and triggers activation of the classical pathway of complement. The crystal structure of the C1q globular domain responsible for its recognition properties has now been solved and refined to 1.9 A of resolution. The structure reveals a compact, almost spherical heterotrimeric assembly held together mainly by non-polar interactions, with a Ca2+ ion bound at the top. The heterotrimeric assembly of the C1q globular domain appears to be a key factor of the versatile recognition properties of this protein. Plausible three-dimensional models of the C1q globular domain in complex with two of its physiological ligands, C-reactive protein and IgG, are proposed, highlighting two of the possible recognition modes of C1q. The C1q/human IgG1 model suggests a critical role for the hinge region of IgG and for the relative orientation of its Fab domain in C1q binding.
==Disease==
Known diseases associated with this structure: C1q deficiency, type A OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120550 120550]], C1q deficiency, type B OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120570 120570]], C1q deficiency, type C OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120575 120575]]


==About this Structure==
==About this Structure==
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[[Category: Pignol, D.]]
[[Category: Pignol, D.]]
[[Category: Verger, D.]]
[[Category: Verger, D.]]
[[Category: CA]]
[[Category: c1q]]
[[Category: c1q]]
[[Category: complement system]]
[[Category: complement system]]
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[[Category: jellyroll]]
[[Category: jellyroll]]


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