THE C-TYPE CARBOHYDRATE-RECOGNITION DOMAIN (CRD) SUPERFAMILY
THE C-TYPE CARBOHYDRATE-RECOGNITION DOMAIN (CRD) SUPERFAMILY
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DOI:
10.1042/bst0220083
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发表时间:
1994-02-01
影响因子:
3.9
通讯作者:
DAY, AJ
中科院分区:
文献类型:
--
作者:
DAY, AJ
The C-type (CaL+-dependent) carbohydrate recognition domain (CRD) is a protein module which is found in a diverse superfamily of proteins involved in a wide range of functions (Figure 1). These functions are mediated by the general property of interacting specifically with carbohydrate structures in a Ca’+-dependent manner. CRDs vary in length from about 11 5 to 130 amino acids and contain four invariant cysteines: disulphide-bonded cysteinelcysteine4 and cysteine2-cysteine3 [11 (see Figure 2). Some CRDs contain two additional disulphidebonded cysteines at the N-terminus (CRDs containing four cysteines are sometimes referred as ‘short-form 0 s’ and those containing six cysteines as ‘long-form CRDs’). CRDs have a characteristic consensus sequence based largely on hydrophobic residues as shown in Figure 2. The proteins of the CRD superfamily can be subdivided into six main groups on the basis of amino acid sequence comparisons of the CRDs [11. The members of the CRD superfamily are shown schematically in Figure 1 with a corresponding multiple sequence alignment in Figure 2. It can be seen that in any particular group the proteins all have the same overall molecular architecture and highly related sequences as well as related functions as will be discussed below.