CTCF binding has been mapped in a number of experimental approaches.
TNF-induced p65 (RELA or NFKB3, an NF-κB subunit) binding has been mapped genome-wide in a number of cells lines (THP-1, HeLa, A549, dendritic cells [ 15, 45, 46]).
Both fibronectin and fibrinogen binding have been mapped to an overlapping domain in LigB comprising repeats 9 11, with repeat 11 possibly enhancing binding by a conformational effect.
P. falciparum IEs from laboratory strains (Ref. 94) and field isolates (Ref. 70) bind to PECAM1 on endothelial cells and the binding site has been mapped to the first four immunoglobulin-like domains of PECAM1 (Ref. 94).
Based on the structural similarity between the crystal structure of the synapsin C domain with ATPases, a highly evolutionary conserved ATP binding site has been mapped in domain C [50], [51] and found to bind ATP with nanomolar affinity in a Ca2+-dependent manner [54].
While the FH binding activity has been mapped to the amino terminal region of CbpA and its allelic variants, multiple regions of human FH have been reported to bind to CbpA, including SCR 6 10, 8 14 and 13 15.
The IGF2-binding domain has been mapped to domain 11, whereas M6P residues bind domains 3 and 9 (Braulke, 1999).
The β-catenin-binding domain has been mapped to amino acid residues 535 636 of mXinα, which overlaps with the known actin binding domains composed of Xin repeats (XR17∼XR19) [1], [5], [7], [9].
Nevertheless, this is the first report that a defined motif of a schistosomal tegument protein with immunoglobulin-binding property has been mapped.
In fact, the Trastuzumab-binding site has been mapped to the C-terminal portion of domain IV in the juxtamembrane region of the ECD (Cho et al, 2003).
In a recent publication, a second talin-binding site has been mapped on the β subunit that, together with the PIPK1γ site, supports the activation of integrin (Wegener et al, 2007).
