4pbp

crystal structure of zebrafish short-chain pentraxin protein

spinqualitylabelsall models 4pbp, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pbp is a 3 chain structure with sequence from Danio rerio. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.648Å Ligands: CA, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CRP_DANRE Displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis, and complement fixation through its calcium-dependent binding to phosphorylcholine.[UniProtKB:P19094] Publication Abstract from PubMed Short-chain pentraxins (PTXs), including CRP and SAP, are innate pattern recognition receptors that play vital roles in the recognition and elimination of various pathogenic bacteria by triggering the classical complement pathway through C1q. Similar to antibodies, pentraxins can also activate opsonisation and phagocytosis by interacting with Fc receptors (FcRs). Various structural studies on human PTXs have been performed, but there are no reports about the crystal structure of bony fish pentraxins. Here, the crystal structures of zebrafish PTX (Dare-PTX-Ca and Dare-PTX) are presented. Both Dare-PTX-Ca and Dare-PTX are cyclic trimers, which are new forms of crystallised pentraxins. The structures reveal that the ligand-binding pocket (LBP) in the recognition face of Dare-PTX is deep and narrow. Homology modelling shows that LBPs from different Dare-PTX loci differ in shape, reflecting their specific recognition abilities. Furthermore, in comparison with the structure of hCPR, a new C1q binding mode was identified in Dare-PTX. In addition, the FcR-binding sites of hSAP are partially conserved in Dare-PTX. These results will shed light on the understanding of a primitive PTX in bony fish, which evolved approximately 450 million years ago. Crystal structures for short-chain pentraxin from zebrafish demonstrate a cyclic trimer with new recognition and effector faces.,Chen R, Qi J, Yuan H, Wu Y, Hu W, Xia C J Struct Biol. 2015 Mar;189(3):259-68. doi: 10.1016/j.jsb.2015.01.001. Epub 2015 , Jan 13. PMID:25592778 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also C-reactive protein

Proteopedia Page Contributors and Editors (what is this?)

OCA