PMID- 8557671
OWN - NLM
STAT- MEDLINE
DCOM- 19960226
LR  - 20210210
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 271
IP  - 2
DP  - 1996 Jan 12
TI  - Structural analysis of monosaccharide recognition by rat liver mannose-binding 
      protein.
PG  - 663-74
AB  - The structural basis of carbohydrate recognition by rat liver mannose-binding 
      protein (MBP-C) has been explored by determining the three-dimensional structure 
      of the C-type carbohydrate-recognition domain (CRD) of MBP-C using x-ray 
      crystallography. The structure was solved by molecular replacement using rat 
      serum mannose-binding protein (MBP-A) as a search model and was refined to 
      maximum Bragg spacings of 1.7 A. Despite their almost identical folds, the 
      dimeric structures formed by the two MBP CRDs differ dramatically. Complexes of 
      MBP-C with methyl glycosides of mannose, N-acetylglucosamine, and fucose were 
      prepared by soaking MBP-C crystals in solutions containing these sugars. 
      Surprisingly, the pyranose ring of mannose is rotated 180 degrees relative to the 
      orientation observed previously in MBP-A, but the local interactions between 
      sugar and protein are preserved. For each of the bound sugars, vicinal, 
      equatorial hydroxyl groups equivalent to the 3- and 4-OH groups of mannose 
      directly coordinate Ca2+ and form hydrogen bonds with residues also serving as 
      Ca2+ ligands. Few interactions are observed between other parts of the sugar and 
      the protein. A complex formed between free galactose and MBP-C reveals a similar 
      mode of binding, with the anomeric hydroxyl group serving as one of the Ca2+ 
      ligands. A second binding site for mannose has also been observed in one of two 
      copies in the asymmetric unit at a sugar concentration of 1.3 M. These structures 
      explain how MBPs recognize a wide range of monosaccharides and suggest how fine 
      specificity differences between MBP-A and MBP-C may be achieved.
FAU - Ng, K K
AU  - Ng KK
AD  - Department of Structural Biology, Stanford University School of Medicine, 
      California 94305, USA.
FAU - Drickamer, K
AU  - Drickamer K
FAU - Weis, W I
AU  - Weis WI
LA  - eng
SI  - PDB/1RDI
SI  - PDB/1RDJ
SI  - PDB/1RDK
SI  - PDB/1RDL
SI  - PDB/1RDM
SI  - PDB/1RDN
SI  - PDB/1RDO
GR  - GM42628/GM/NIGMS NIH HHS/United States
GR  - GM50565/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Carrier Proteins)
RN  - 0 (Mannose-Binding Lectins)
RN  - 0 (Monosaccharides)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Carbohydrate Sequence
MH  - Carrier Proteins/*metabolism
MH  - Crystallization
MH  - Crystallography, X-Ray
MH  - Liver/*metabolism
MH  - Mannose-Binding Lectins
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Molecular Structure
MH  - Monosaccharides/*metabolism
MH  - Protein Conformation
MH  - Rats
EDAT- 1996/01/12 00:00
MHDA- 1996/01/12 00:01
CRDT- 1996/01/12 00:00
PHST- 1996/01/12 00:00 [pubmed]
PHST- 1996/01/12 00:01 [medline]
PHST- 1996/01/12 00:00 [entrez]
AID - S0021-9258(18)95485-2 [pii]
AID - 10.1074/jbc.271.2.663 [doi]
PST - ppublish
SO  - J Biol Chem. 1996 Jan 12;271(2):663-74. doi: 10.1074/jbc.271.2.663.