PMID- 10207177
OWN - NLM
STAT- MEDLINE
DCOM- 19990607
LR  - 20190513
IS  - 0959-6658 (Print)
IS  - 0959-6658 (Linking)
VI  - 9
IP  - 5
DP  - 1999 May
TI  - Oligosaccharide analysis and molecular modeling of soluble forms of glycoproteins
      belonging to the Ly-6, scavenger receptor, and immunoglobulin superfamilies
      expressed in Chinese hamster ovary cells.
PG  - 443-58
AB  - Most cell surface molecules are glycoproteins consisting of linear arrays of
      globular domains containing stretches of amino acid sequence with similarities to
      regions in other proteins. These conserved regions form the basis for the
      classification of proteins into superfamilies. Recombinant soluble forms of six
      leukocyte antigens belonging to the Ly-6 (CD59), scavenger receptor (CD5), and
      immunoglobulin (CD2, CD48, CD4, and Thy-1) superfamilies were expressed in the
      same Chinese hamster ovary cell line, thus providing an opportunity to examine
      the extent to which N-linked oligosaccharide processing might vary in a
      superfamily-, domain-, or protein-dependent manner in a given cell. While we
      found no evidence for superfamily-specific modifications of the glycans, marked
      differences were seen in the types of oligosaccharides attached to individual
      proteins within a given superfamily. The relative importance of local protein
      surface properties versus the overall tertiary structure of the molecules in
      directing this protein-specific variation was examined in the context of
      molecular models. These were constructed using the 3D structures of the proteins,
      glycan data from this study, and an oligosaccharide structural database. The
      results indicated that both the overall organization of the domains and the local
      protein structure can have a large bearing on site-specific glycan modification
      of cells in stasis. This level of control ensures that the surface of a single
      cell will display a diverse repertoire of glycans and precludes the presentation 
      of multiple copies of a single oligosaccharide on the cell surface. The glycans
      invariably shield large regions of the protein surfaces although, for the
      glycoproteins examined here, these did not hinder the known active sites of the
      molecules. The models also indicated that sugars are likely to play a role in the
      packing of the native cell surface glycoproteins and to limit nonspecific
      protein-protein interactions. In addition, glycans located close to the cell
      membrane are likely to affect crucially the orientation of the glycoproteins to
      which they are attached.
FAU - Rudd, P M
AU  - Rudd PM
AD  - Glycobiology Institute, Department of Biochemistry, University of Oxford, South
      Parks Road, Oxford OX1 3QU, UK.
FAU - Wormald, M R
AU  - Wormald MR
FAU - Harvey, D J
AU  - Harvey DJ
FAU - Devasahayam, M
AU  - Devasahayam M
FAU - McAlister, M S
AU  - McAlister MS
FAU - Brown, M H
AU  - Brown MH
FAU - Davis, S J
AU  - Davis SJ
FAU - Barclay, A N
AU  - Barclay AN
FAU - Dwek, R A
AU  - Dwek RA
LA  - eng
GR  - Wellcome Trust/United Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Glycobiology
JT  - Glycobiology
JID - 9104124
RN  - 0 (Antigens, CD)
RN  - 0 (Antigens, Differentiation)
RN  - 0 (Antigens, Ly)
RN  - 0 (CD2 Antigens)
RN  - 0 (CD4 Antigens)
RN  - 0 (CD48 Antigen)
RN  - 0 (CD48 protein, human)
RN  - 0 (Cd48 protein, mouse)
RN  - 0 (Cd48 protein, rat)
RN  - 0 (Glycoproteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Oligosaccharides)
RN  - 0 (Receptors, Immunologic)
RN  - 0 (Receptors, Lipoprotein)
RN  - 0 (Receptors, Scavenger)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Scarb1 protein, mouse)
RN  - 0 (Scavenger Receptors, Class B)
RN  - 0 (Thy-1 Antigens)
SB  - IM
MH  - Animals
MH  - Antigens, CD/chemistry
MH  - Antigens, Differentiation/*chemistry/metabolism
MH  - Antigens, Ly/chemistry
MH  - CD2 Antigens/chemistry
MH  - CD4 Antigens/chemistry
MH  - CD48 Antigen
MH  - CHO Cells
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Cricetinae
MH  - Glycoproteins/*chemistry/metabolism
MH  - Glycosylation
MH  - Humans
MH  - *Membrane Proteins
MH  - *Models, Molecular
MH  - Molecular Sequence Data
MH  - Oligosaccharides/*analysis
MH  - Protein Conformation
MH  - Protein Processing, Post-Translational
MH  - Protein Structure, Secondary
MH  - Rats
MH  - Receptors, Immunologic/chemistry
MH  - *Receptors, Lipoprotein
MH  - Receptors, Scavenger
MH  - Recombinant Proteins/chemistry/metabolism
MH  - Scavenger Receptors, Class B
MH  - Thy-1 Antigens/chemistry
EDAT- 1999/04/20 00:00
MHDA- 1999/04/20 00:01
CRDT- 1999/04/20 00:00
PHST- 1999/04/20 00:00 [pubmed]
PHST- 1999/04/20 00:01 [medline]
PHST- 1999/04/20 00:00 [entrez]
AID - cwc034 [pii]
AID - 10.1093/glycob/9.5.443 [doi]
PST - ppublish
SO  - Glycobiology. 1999 May;9(5):443-58. doi: 10.1093/glycob/9.5.443.