# STRUCTURE AND INTERACTION OF PROTEINS WITH MEMBRANES

> **NIH NIH R01** · VIRGINIA COMMONWEALTH UNIVERSITY · 1988 · $113,732

## Abstract

Interaction of external protein ligands with sugar bearing membrane
receptors are known to trigger many cellular processes.  This proposal
addresses the specific question of the stereochemical requirements that
lead to productive protein-cell surface receptor complex formation.
Lectin-sugar complexes have served as useful biological model systems to
answer this question.  Such answers require solid structural knowledge of
both lectin and receptor on the atomic level in order to be definitive.

Wheat germ agglutinin (WGA) is one of the most thoroughly studied lectins
and known to specifically interact with sialic acid bearing receptor
glycoproteins on eukaryotic cell membranes, thereby causing numerous
effects such as cytotoxicity or morphological restriction.  Two closely
homologous molecular forms of this lectin (isolectins 1 and 2) are being
studied in atomic detail by x-ray crystallographic and chemical
techniques.  Knowledge obtained from the recently determined high
resolution structure (1.8A) of isolectin 2 will be used in continuing
studies to refine the crystal structure of isolectin 1 at 2.0A resolution
and to determine the structure of the isolectin 1/N-acetyl neuraminyl
lactose complex at 2.2A.  The structure of this complex will subsequently
be compared with the analogous one of isolectin 2 (2.2A) to explain their
differential saccharide binding affinities.

We also propose to determine the crystal structure of a compl x of WGA with
a sialoglycopeptide (T-5) derived from the major red cell membrane protein
glycophorin A, a specific receptor for WGA.  This will be done by a
combination of the methods of heavy atom isomorphous replacement and
molecular replacement.  Using the refined WGA structure it will be possible
to analyze in detail the stereochemistry of this complex and determine the
extent to which carbohydrate and peptide interact with the lectin surface.
The structure of this complex will be a more definitive model for
protein-cell surface saccharide interactions than are the simple
saccharide/WGA complexes explored up to now.

## Key facts

- **NIH application ID:** 3127604
- **Project number:** 5R01AI017992-08
- **Recipient organization:** VIRGINIA COMMONWEALTH UNIVERSITY
- **SAM.gov UEI:** MLQFL4JSSAA9
- **Principal Investigator:** CHRISTINE S WRIGHT
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1988
- **Award amount:** $113,732
- **Award type:** 5
- **Project period:** 1980-09-01 → 1992-03-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3127604

## Citation

> US National Institutes of Health, RePORTER application 3127604, STRUCTURE AND INTERACTION OF PROTEINS WITH MEMBRANES (5R01AI017992-08). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3127604. Licensed CC0.

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