Accession Number:

ADA239041

Title:

A Modular Approach to Protein Design.

Descriptive Note:

Final rept 1 Feb 88-30 Jun 91,

Corporate Author:

ROCHESTER UNIV NY

Personal Author(s):

Report Date:

1991-07-18

Pagination or Media Count:

6.0

Abstract:

We have taken a modular approach to study peptide interactions with proteins as a model for protein-protein interactions. Two basic approaches were applied to this problem, and peptides were designed to bind either a specific sequence of double stranded DNA or the PP56lck tyrosine protein kinase. This protein kinase likely is the cytoplasmic effector of CD4, a transmembrane receptor whose aviation in vivo is associated with an increase in cytoplasmic free calcium. Peptides have been synthesized which bind to each of these macromolecules with KDs near 2mM. In addition to binding pp56lck tightly, one peptide has been found to stimulate the activity of this enzyme up to 20-fold. We have shown that ionic interactions are important for this activation, and that these peptides alter the substrate specificity of this enzyme. Due to our greater success with the protein kinase project, we have recently been concentrating our efforts on this project.

Subject Categories:

  • Medicine and Medical Research

Distribution Statement:

APPROVED FOR PUBLIC RELEASE