Acquisition of ordered conformation by the N-terminal domain of the human small proline rich 2 protein

Eleonora Candi, Gerry Melino, Marco Sette, Sergio Oddi, Pietro Guerrieri, Maurizio Paci

Research output: Contribution to journalArticlepeer-review


The cornified cell envelope (CE) is a crucial structure for barrier function in terminally differentiated dead stratified squamous epithelia. It is assembled by transglutaminase enzymes (TGases) that cross-link several proteins such as loricrin and the small proline rich (SPR) proteins. Human SPR2 protein is crosslinked with widely differing efficiencies by TGases 1, 2, and 3 using exclusively residues in the N- and C-terminal domains. In order to understand if the absence of the cross-linking catalyzed by TGases in the central domain is due to the conformation adopted, we have investigated the structural properties in solution of three peptides that correspond to the N-terminal domain, to three repeats of the central domain, and to the C-terminal domain. Together, the NMR and CD data strongly indicate the presence of a highly flexible non α-helix, non β-sheet structure in SPR2. Thus, SPR2 appears to function as a flexible cross-bridging protein to provide tensile strength or rigidity to the CE of the stratified squamous epithelia in which it is expressed.

Original languageEnglish
Pages (from-to)395-400
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - Aug 27 1999


  • Barrier function
  • Cornified envelope
  • Nuclear magnetic resonance
  • Small proline-rich protein

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


Dive into the research topics of 'Acquisition of ordered conformation by the N-terminal domain of the human small proline rich 2 protein'. Together they form a unique fingerprint.

Cite this