PMID- 24150739
OWN - NLM
STAT- MEDLINE
DCOM- 20140926
LR  - 20211021
IS  - 1573-4986 (Electronic)
IS  - 0282-0080 (Linking)
VI  - 31
IP  - 1
DP  - 2014 Jan
TI  - Effect of distal sugars and interglycosidic linkage on the N-glycoprotein linkage 
      region conformation: synthesis and X-ray crystallographic investigation of 
      beta-1-N-alkanamide derivatives of cellobiose and maltose as disaccharide analogs of 
      the conserved chitobiosylasparagine linkage.
PG  - 71-87
LID - 10.1007/s10719-013-9504-8 [doi]
AB  - The linkage region constituents, 2-deoxy-2-acetamido-beta-D-glucopyranose (GlcNAc) 
      and L-asparagine (Asn) are conserved in the N-glycoproteins of all eukaryotes. 
      Elucidation of the structure and conformation of the linkage region of 
      glycoproteins is important to understand the presentation and dynamics of the 
      carbohydrate chain at the protein/cell surface. Earlier crystallographic studies 
      using monosaccharide models and analogs of N-glycoprotein linkage region have 
      shown that the N-glycosidic torsion, varphiN, is more influenced by the structural 
      variation in the sugar part than that of the aglycon moiety. To access the 
      influence of distal sugar as well as interglycosidic linkage (alpha or beta) on the 
      N-glycosidic torsion angles, cellobiosyl and maltosyl alkanamides have been 
      synthesized and structural features of seven of these analogs have been 
      characterized by X-ray crystallography. Comparative analysis of the seven 
      disaccharide analogs with the reported monosaccharide analogs showed that the varphiN 
      value of cellobiosyl analogs deviate ~9 degrees  with respect to GlcbetaNHAc. In the case of 
      maltosyl analogs, deviation is more than 18 degrees . These deviations indicate that the 
      N-glycosidic torsion is influenced by addition of distal sugar as well as with 
      respect to inter glycosidic linkage (alpha or beta); it is less influenced by changes 
      occurring at the aglycon. The chi(2) value of alkanamide derived from glucose, 
      cellobiose and maltose exhibit a large range of variations (from 1.6 degrees  to 
      -109.9 degrees ). This large span of chi(2) value suggests the greater degree of rotational 
      freedom around C1'-C2' bond which is restricted in GlcNAc alkanamides. The 
      present finding explicitly proved the importance of molecular architecture in the 
      N-glycoproteins linkage region to maintain the linearity, planarity and rigidity. 
      These factors are necessary for N-glycan to serve role in inter- as well as 
      intramolecular carbohydrate-protein interactions.
FAU - Mathiselvam, Manoharan
AU  - Mathiselvam M
AD  - Department of Chemistry, Indian Institute of Technology Madras, Chennai, 600036, 
      India, mathi24@gmail.com.
FAU - Ramkumar, Venkatachalam
AU  - Ramkumar V
FAU - Loganathan, Duraikkannu
AU  - Loganathan D
FAU - Perez, Serge
AU  - Perez S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20131023
PL  - United States
TA  - Glycoconj J
JT  - Glycoconjugate journal
JID - 8603310
RN  - 0 (Glycoproteins)
RN  - 16462-44-5 (Cellobiose)
RN  - 69-79-4 (Maltose)
SB  - IM
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Cellobiose/*chemistry
MH  - Crystallography, X-Ray
MH  - Glycoproteins/*chemistry
MH  - Maltose/*chemistry
MH  - Molecular Sequence Data
EDAT- 2013/10/24 06:00
MHDA- 2014/09/27 06:00
CRDT- 2013/10/24 06:00
PHST- 2013/08/25 00:00 [received]
PHST- 2013/10/07 00:00 [accepted]
PHST- 2013/10/07 00:00 [revised]
PHST- 2013/10/24 06:00 [entrez]
PHST- 2013/10/24 06:00 [pubmed]
PHST- 2014/09/27 06:00 [medline]
AID - 10.1007/s10719-013-9504-8 [doi]
PST - ppublish
SO  - Glycoconj J. 2014 Jan;31(1):71-87. doi: 10.1007/s10719-013-9504-8. Epub 2013 Oct 
      23.