Legume lectin structure

被引:458
作者
Loris, R [1 ]
Hamelryck, T [1 ]
Bouckaert, J [1 ]
Wyns, L [1 ]
机构
[1] Free Univ Brussels VIB, Lab Ultrastruktuur, B-1640 Rhode St Genese, Belgium
来源
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1998年 / 1383卷 / 01期
关键词
lectin; protein-carbohydrate interactions; quaternary structure; carbohydrate recognition;
D O I
10.1016/S0167-4838(97)00182-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The legume lectins are a large family of homologous carbohydrate binding proteins that are found mainly in the seeds of most legume plants. Despite their strong similarity on the level of their amino acid sequences and tertiary structures, their carbohydrate specificities and quaternary structures vary widely. In this. review we will focus on the structural features of legume lectins and their complexes with carbohydrates. These will be discussed in the light of recent mutagenesis results when appropriate. Monosaccharide specificity seems to be achieved by the use of a conserved core of residues that hydrogen bond to the sugar, and a variable loop that determines the exact shape of the monosaccharide binding site. The higher affinity for particular oligosaccharides and monosaccharides containing a hydrophobic aglycon results mainly from a few distinct subsites next to the monosaccharide binding site. These subsites consist of a small number of variable residues and are found in both the mannose and galactose specificity groups. The quaternary structures of these proteins form the basis of a higher level of specificity, where the spacing between individual epitopes of multivalent carbohydrates becomes important. This results in homogeneous cross-linked lattices even in mixed precipitation systems, and is of relevance for their effects on the biological activities of cells such as mitogenic responses. Quaternary structure is also thought to play an important role in the high affinity interaction between some legume lectins and adenine and a series of adenine-derived plant hormones. The molecular basis of the variation in quarternary structure in this group of proteins is poorly understood. (C) 1997 Elsevier Science B.V.
引用
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页码:9 / 36
页数:28
相关论文
共 157 条
[1]  
ABE Y, 1993, J BIOL CHEM, V268, P3525
[2]  
ACHARYA S, 1990, J BIOL CHEM, V265, P11586
[3]   Mutational studies of the amino acid residues in the combining site of Erythrina corallodendron lectin [J].
Adar, R ;
Sharon, N .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1996, 239 (03) :668-674
[4]  
ANIMASHAUN T, 1989, J BIOL CHEM, V264, P4657
[5]   MODIFICATION BY SITE-DIRECTED MUTAGENESIS OF THE SPECIFICITY OF ERYTHRINA-CORALLODENDRON LECTIN FOR GALACTOSE DERIVATIVES WITH BULKY SUBSTITUENTS AT C-2 [J].
ARANGO, R ;
RODRIGUEZARANGO, E ;
ADAR, R ;
BELENKY, D ;
LOONTIENS, FG ;
ROZENBLATT, S ;
SHARON, N .
FEBS LETTERS, 1993, 330 (02) :133-136
[6]   A STRUCTURAL COMPARISON OF CONCANAVALIN-A AND TOMATO BUSHY STUNT VIRUS PROTEIN [J].
ARGOS, P ;
TSUKIHARA, T ;
ROSSMANN, MG .
JOURNAL OF MOLECULAR EVOLUTION, 1980, 15 (03) :169-179
[7]  
BAEZINGER JU, 1979, J BIOL CHEM, V254, P2400
[8]   CRYSTAL-STRUCTURE OF PEANUT LECTIN, A PROTEIN WITH AN UNUSUAL QUATERNARY STRUCTURE [J].
BANERJEE, R ;
MANDE, SC ;
GANESH, V ;
DAS, K ;
DHANARAJ, V ;
MAHANTA, SK ;
SUGUNA, K ;
SUROLIA, A ;
VIJAYAN, M .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1994, 91 (01) :227-231
[9]   Conformation, protein-carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin-lactose complex [J].
Banerjee, R ;
Das, K ;
Ravishankar, R ;
Suguna, K ;
Surolia, A ;
Vijayan, M .
JOURNAL OF MOLECULAR BIOLOGY, 1996, 259 (02) :281-296
[10]   PRECIPITATION OF CONCANAVALIN A BY A HIGH MANNOSE TYPE GLYCOPEPTIDE [J].
BHATTACHARYYA, L ;
BREWER, CF .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1986, 137 (02) :670-674