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A hypothetical structural role for proline residues in the flanking segments of protein-protein interaction sites.

Abstract：

:An examination of more than 1600 protein-protein interaction sites indicated that proline is the residue most commonly found near interaction sites. A structural role is distinguished for these proline residues in the flanking segments of protein-protein interaction sites. The unique nature of proline helps protect the integrity and present the sites, thus promoting protein-protein interactions. A novel approach to the design and development of potent peptide drugs and a simple predictive method to identify protein-protein interaction sites directly from the amino acid sequence have been developed based on this finding. The recognition of this structural role for proline has strong implications for protein chemistry and protein engineering.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Kini RM,Evans HJ

doi

10.1006/bbrc.1995.2084

subject

Has Abstract

pub_date

1995-07-26 00:00:00

pages

1115-24

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(85)72084-0

journal_volume

212

pub_type

杂志文章

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