Accession Number:

ADA209370

Title:

Protein Structure and Function: Design and Synthesis of Peptide Recognition Sequences

Descriptive Note:

Annual rept. 1 May 1988-15 Jun 1989

Corporate Author:

JOHNS HOPKINS UNIV BALTIMORE MD DEPT OF PHARMACOLOGY

Personal Author(s):

Report Date:

1989-06-15

Pagination or Media Count:

11.0

Abstract:

The goal of this research is to characterize the chemical and physical properties that define the interactions between the Arg-Gly-Asp RGD recognition sequence of protein adhesion molecules and their cellular receptors. NMR analysis of the solution conformation of the pentapeptide ligand GRGDS indicate a folded structure of the molecule in solution with a type II B-turn in which the amide carboxyl oxygen of Arg-2 receives a hydrogen bond from the amide NH of Ser-5. These studies are now being extended with a 14 residue ligand to test the role of the carboxylate and amino termini of the short peptide. The conformations of RGD peptides has also been analyzed by molecular mechanics and Monte Carlo methods. The predicted structure of the GRGDS molecule correspond to most of the NOE data. Studies of RGD binding proteins has led to the identification of a cell adhesion receptor corresponding to the Pgp-1CD44 HermesSCMRIII family of molecules that are implicated in a variety of cell-cell adhesion processes. The cDNA of this protein has been isolated and sequenced and the molecule is being utilized as a possible in vitro model of RGD ligand- receptor binding. Keywords Molecular biology Receptor sites Binding sites Synthesis.

Subject Categories:

  • Genetic Engineering and Molecular Biology

Distribution Statement:

APPROVED FOR PUBLIC RELEASE