Heparin sequence

Conformational analysis of longer regular heparin sequences " gives evidence for regular arrays of three sulfate groups alternating on both sides of a helix... 

Fig. 5. Hidden protein-binding sequences in HS. (o) Two different proteins bind to the same, fully sulfated ( regular ) heparin sequence. (Z>) The same proteins interact specifically each with one distinct HS sequence. The symbols are the same as in Fig. 1. For further information see the text.

Heparin Analytical Tool. Recently, a heparin sequencing technology called property-encoded nomenclature/MALDI sequencing was developed (173). 

Nugent MA. Heparin sequencing brings structure to the function of complex oligosaccharides. Proc Natl Acad Sci USA 2000 97 10301-10303. 

AT-III. Therefore, the different affinities of isolated fragments to AT-III respond to different degrees of pentasaccharide abundance. The heparin sequences were printed on amine-coated slides to prepare the corresponding heparin chips whose utility was demonstrated by incubation with proteins such as AT-III, FGF-1, and FGF-2. Interestingly, the results obtained after AT-III incubation were in agreement with those obtained by using affinity chromatography on AT-III that served to classify the sequences. 

Margalit H. Fisher N. Ben-Sasson S.A. (1993) Comparative analysis of structurally defined heparin binding sequences reveals a distinct spatial distribution of basic residues // J. Biol. Chem V. 268. P.19228-19231. 

Figure 48-3. Schematic representation of fibronectin. Seven functional domains of fibronectin are represented two different types of domain for heparin, cell-binding, and fibrin are shown. The domains are composed of various combinations of three structural motifs (I, II, and III), not depicted in the figure. Also not shown is the fact that fibronectin is a dimer joined by disulfide bridges near the carboxyl terminals of the monomers. The approximate location of the RGD sequence of fibronectin, which interacts with a variety of fibronectin integrin receptors on cell surfaces, is indicated by the arrow. (Redrawn after Yamada KM Adhesive recognition sequences.

Figure 48-9. Structure of heparin. The polymer section illustrates structural features typical of heparin however, the sequence of variously substituted repeating disaccharide units has been arbitrarily selected. In addition, non-O-sulfated or 3-0-sulfated glucosamine residues may also occur. (Modified, redrawn, and reproduced, with permission, from Lindahl U et al Structure and biosynthesis of heparin-like polysaccharides. Fed Proc 1977 36 19.)...

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