Lectins crystal structure

Fig. B.5.2. Crystal structure of an a-D-mannose unit bound to the C-type lectin rat mannose-binding protein A (MBP-A,...

Llera, A. S., Viedma, F., Sanchez-Madrid, F., and Tormo, J. (2001). Crystal structure of the C-type lectin-like domain from the human hematopoietic cell receptor CD69. /. Biol. Chem. 276(10), 7312-7319. 

C.S. Wright. 1992. Crystal structure of a wheat germ agglutinin/ glycophorin-sialoglycopeptide receptor complex Structural basis for cooperative lectin-cell binding J Biol. Chem. 267 14345-14352. (PubMed)... 

The conserved sequences and available X-ray crystal structures of C-type lectin CRDs correlate with a common structural motif identified in rat serum mannose-binding protein-A (MBP-A) as represented in O Fig. 2 [19,20]. There are two a-helices, 6 /3-strands, and 2 disulfide bonds common to this motif. Divalent cation binding sites are located in the loop regions. 

X-ray crystal structures of the lectin domains of human and bovine galectin 1, galectin 10 and similar domains from other proteins. (Reproduced with permission from [181])... 

Quesenbeny and Drickamer. and by comparison to die crystal structure of rat mannose binding protein (MBP), a C-type lectin related to the selectins. ... 

Krauspenhaar, R., Eschenburg, S., Perbandt, M., Kornilov, V., Konareva, N., Mikailova, L, Stoeva, S., Wacker, R., Maier, T., Singh, T., Mikhailov, A., Voelter, W. and Betzel, C. (1999) Crystal structure of mistletoe lectin I from Viscum album. Biochem Biophys Res Commun, 257, 418 24. 

A listing of the X-ray crystal structure (arranged in chronological order) of plant lectins is presented in Table 2 commencing with the structure of concanavalin A at 3 A resolution [38,39]. Interestingly, it was not until 1989 that a definitive high resolution X-ray crystal structure of the concanavalin A-methyl a-D-mannopyranoside complex was elucidated [40], and the most recently reported is that of peanut agglutinin [41]. Reviews on carbohydrate-protein interactions are also worthy of note [42-45]. 

The X-ray crystal structure of the pea lectin bound to the branched trimannosyl core oligosaccharide found in N-linked glycoproteins was solved at 2.6 A resolution [49]. It... 

Without doubt, concanavalin A (Con A) is the most celebrated and has proven to be one of the most useful of the plant lectins. Its physical chemical properties and carbohydratebinding properties are well documented in previous reviews [3,8]. Suffice it to note that it was first isolated and crystallized by Sumner and Howell in 1936, who showed it to require metal ions for its activity [74]. By virtue of its interaction with branched a-D-glucans, it is readily prepared by affinity chromatography on crossed-linked dextran (Sephadex) [75, 76]. A homotetramer at pH 7 (subunit M, = 26 500 Da) of Con A has been sequenced [77] and its crystal structure determined both in its native form [38,39] and complexed with methyl a-D-mannopyranoside [40] and Man(al-3)[Man(al-6)]Man[49]. 

The X-ray crystal structure of the pea lectin has been determined at 2 A [48,49], The molecule is peanut-shaped and strikingly similar to the Con A dimer with a high content of 3-structure. The heterotetramer contains two non-interacting binding sites per molecule [87]. 

The recent solution of the crystal structure of a dimeric form of pertussis toxin provided support for the composite nature of the molecule [124]. Thus, the WGA-like region of S2 superimposes on the homologous part of the three-dimensional structure of WGA (residues 62-67), while the segment homologous to the C-type lectins superimposes on the core of rat mannose binding protein, a C-type lectin. 

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