Expert Reviews in Molecular Medicine: http://www-ermm.cbcu.cam.ac.uk
Accession information: (01)00331-3h.htm (shortcode: fig001mfh); 18 July 2001
Schematic illustrations of the major secondary structural motifs of the four chemokine subfamilies
Mitchell J. Frederick and Gary L. Clayman
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Figure 1. Schematic illustrations of the major secondary structural motifs of the four chemokine subfamilies. In each of the four subfamilies (a–d), the N-terminus (NH2) is followed by a small stretch of disordered structure (thin black wavy line). After the second conserved cysteine residue (C in red) in the first three subfamilies (a–c), there is a small loop ending in a single turn of an alpha helix (pink Z shape), which is then followed by three anti-parallel beta sheets (thick magenta arrows) separated by turns and loops (thin black curved lines). In the first three subfamilies, an alpha helix (purple zigzag) occurs near the C-terminus (COOH) and is followed by another disordered region (black). Disulphide bonds between the conserved cysteine residues are represented by a dashed green line. The CXXXC chemokine is exceptional compared with the other subfamilies in that it can occur as a transmembrane protein as shown, or as a soluble molecule following cleavage (not shown). A mucin domain, which extends the CXXXC chemokine away from the cell membrane, is depicted as a blue branched structure, and the transmembrane region and cytoplasmic carboxyl tail are also shown. The structure of the C chemokine (d) is mostly drawn with dotted lines, because it is largely unknown (fig001mfh).
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