This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3dpa
From Proteopedia
CRYSTAL STRUCTURE OF CHAPERONE PROTEIN PAPD REVEALS AN IMMUNOGLOBULIN FOLD
Overview
The chaperone protein PapD mediates assembly of pili in Escherichia coli. Its polypeptide chain folds into two immunoglobulin-type domains that are homologous in sequence to the human lymphocyte differentiation antigen Leu-1/CD5.
About this Structure
3DPA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of chaperone protein PapD reveals an immunoglobulin fold., Holmgren A, Branden CI, Nature. 1989 Nov 16;342(6247):248-51. PMID:2478891 Page seeded by OCA on Sun May 4 22:00:25 2008
