Solution structure of the glycosylphosphatidylinositol membrane anchor glycan of Trypanosoma brucei variant surface glycoprotein

Journal Article · Tue Apr 04 04:00:00 EDT 1989 · Biochemistry; (USA)

DOI:https://doi.org/10.1021/bi00433a020· OSTI ID:5476912

Homans, S W; Edge, C J; Ferguson, M A.J.; Dwek, R A; Rademacher, T W ^[1]

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1. Oxford Univ. (England)

The average solution conformation of the glycosylphosphatidylinositol (GPI) membrane anchor of Trypanosoma brucei variant surface glycoprotein (VSG) has been determined by using a combination of two-dimensional {sup 1}H-{sup 1}H NMR methods together with molecular orbital calculations and restrained molecular dynamics simulations. This allows the generation of a model to describe the orientation of the glycan with respect to the membrane. This shows that the glycan exists in an extended configuration along the plane of the membrane and spans an area of 600 {angstrom}{sup 2}, which is similar to the cross-sectional area of a monomeric N-terminal VSG domain. Taken together, these observations suggest a possible space-filling role for the GPI anchor that may maintain the integrity of the VSG coat. The potential importance of the GPI glycan as a chemotherapeutic target is discussed in light of these observations.

• OSTI ID: 5476912
• Journal Information: Biochemistry; (USA), Journal Name: Biochemistry; (USA) Vol. 28:7; ISSN 0006-2960; ISSN BICHA
• Country of Publication: United States
• Language: English

Related Subjects

550601* -- Medicine-- Unsealed Radionuclides in Diagnostics
62 RADIOLOGY AND NUCLEAR MEDICINE
ANIMALS
AQUEOUS SOLUTIONS
BARYONS
CARBOHYDRATES
CONFORMATIONAL CHANGES
DISPERSIONS
ELEMENTARY PARTICLES
ESTERS
FERMIONS
GLUCOPROTEINS
GLYCOPROTEINS
HADRONS
INVERTEBRATES
LIFE CYCLE
LIPIDS
MAGNETIC RESONANCE
MASTIGOPHORA
MEMBRANES
MICROORGANISMS
MIXTURES
MOLECULAR STRUCTURE
NUCLEAR MAGNETIC RESONANCE
NUCLEONS
ORGANIC COMPOUNDS
ORGANIC PHOSPHORUS COMPOUNDS
PARASITES
PHOSPHOLIPIDS
PROTEINS
PROTONS
PROTOZOA
RESONANCE
SACCHARIDES
SOLUTIONS
TRYPANOSOMA