The whey acidic protein family

A new signature motif and three-dimensional structure by comparative modeling

Shoba Ranganathan*, Kaylene J. Simpson, Denis C. Shaw, Kevin R. Nicholas

*Corresponding author for this work

Research output: Contribution to journalArticle

122 Citations (Scopus)

Abstract

Whey acidic proteins (WAP) from the mouse, rat, rabbit, camel, and pig comprise two "fonr-disnlfide core" domains. From a detailed analysis of all sequences containing this domain, we propose a new PROSITE motif ([KRHGVLN]X-{PFj-X-[CF]-[PQSVLI]-X(9,19)-C-(P}-X-[DN]-X-/N}[CE]-X(5)-C-C) to accurately identify new fonr-disitlflde core proteins. A consensus model for the WAP proteins is proposed, based on the human mucous proteinase inhibitor crystal structure. This article presents a detailed atomic model for the two-domain porcine WAP sequence by comparative modeling. Surface electrostatic potential calculations indicate that the second domain of the pig WAP model is similar to the functional human mucous proteinase inhibitor domains, whereas the first domain may be nonfunctional.

Original languageEnglish
Pages (from-to)106-113
Number of pages8
JournalJournal of Molecular Graphics and Modelling
Volume17
Issue number2
Publication statusPublished - Apr 1999
Externally publishedYes

Keywords

  • Four-disitlflde core
  • Molecular electrostatic potential
  • Molecular model
  • Sequence motifs
  • Sequence-structure comparison
  • WAP

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