PMID- 7711015
OWN - NLM
STAT- MEDLINE
DCOM- 19950517
LR  - 20231213
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 34
IP  - 15
DP  - 1995 Apr 18
TI  - X-ray crystal structure of the soybean agglutinin cross-linked with a biantennary 
      analog of the blood group I carbohydrate antigen.
PG  - 4933-42
AB  - Soybean agglutinin (SBA) (Glycine max), which is a tetrameric GalNAc/Gal-specific 
      lectin, has recently been reported to form unique, highly organized cross-linked 
      complexes with a series of naturally occurring and synthetic multiantennary 
      carbohydrates with terminal GalNAc or Gal residues [Gupta, D., Bhattacharyya, L., 
      Fant, J., Macaluso, F., Sabesan, S., & Brewer, C. F. (1994) Biochemistry 33, 
      7495-7504]. In order to elucidate the nature of these complexes, the X-ray 
      crystallographic structure of SBA cross-linked with a biantennary analog of the 
      blood group I carbohydrate antigen is reported. The structure reveals that 
      lattice formation is promoted uniquely by the bridging action of the bivalent 
      pentasaccharide (beta-LacNAc)2Gal-beta-R, where R is -O(CH2)5COOCH3 and the 
      beta-LacNAc moieties are linked to the 2 and 6 positions of the core Gal. The 
      structure of SBA complexed with the synthetic biantennary pentasaccharide has 
      thus been determined by molecular replacement techniques and refined at 2.6 A 
      resolution to an R value of 20.1%. The crystals are hexagonal with a P6(4)22 
      space group, which differs significantly from that of crystals of the free 
      protein. In the structure, each monomeric asymmetric unit contains a Man9 
      oligomannose-type chain at Asn 75, with only the first two GlcNAc residues 
      visible. The overall tertiary structure of the SBA subunit is similar to that of 
      other legume lectins as well as certain animal lectins. However, the dimer 
      interface in the SBA tetramer is unusual in that only one complete peptide chain 
      is sterically permitted, thus requiring juxtapositioning of one C-terminal 
      fragmented subunit together with an intact subunit. Association between SBA 
      tetramers involves binding of the terminal Gal residues of the pentasaccharide at 
      identical sites in each monomer, with the sugar cross-linking to a 
      symmetry-related neighbor molecule. The cross-linking pentasaccharide is in a 
      conformation that possesses a pseudo-2-fold axis of symmetry which lies on a 
      crystallographic 2-fold axis of symmetry of the lattice. Hence, the symmetry 
      properties of the bivalent oligosaccharide as well as the lectin are structural 
      determinants of the lattice. The results are discussed in terms of 
      multidimensional carbohydrate-lectin cross-linked complexes, as well as the 
      signal transduction properties of multivalent lectins.
FAU - Dessen, A
AU  - Dessen A
AD  - Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 
      10461, USA.
FAU - Gupta, D
AU  - Gupta D
FAU - Sabesan, S
AU  - Sabesan S
FAU - Brewer, C F
AU  - Brewer CF
FAU - Sacchettini, J C
AU  - Sacchettini JC
LA  - eng
GR  - CA-16054/CA/NCI NIH HHS/United States
GR  - GM-47637/GM/NIGMS NIH HHS/United States
GR  - P30 CA-13330/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (I Blood-Group System)
RN  - 0 (Isoantigens)
RN  - 0 (Lectins)
RN  - 0 (Plant Lectins)
RN  - 0 (Soybean Proteins)
RN  - 0 (soybean lectin)
SB  - IM
MH  - Binding Sites
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Crystallization
MH  - Crystallography, X-Ray
MH  - I Blood-Group System/*immunology
MH  - Isoantigens/*chemistry
MH  - Lectins/*chemistry
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Plant Lectins
MH  - Protein Binding
MH  - Protein Conformation
MH  - *Soybean Proteins
MH  - Glycine max
EDAT- 1995/04/18 00:00
MHDA- 1995/04/18 00:01
CRDT- 1995/04/18 00:00
PHST- 1995/04/18 00:00 [pubmed]
PHST- 1995/04/18 00:01 [medline]
PHST- 1995/04/18 00:00 [entrez]
AID - 10.1021/bi00015a004 [doi]
PST - ppublish
SO  - Biochemistry. 1995 Apr 18;34(15):4933-42. doi: 10.1021/bi00015a004.