The whey acidic protein family: a new signature motif and three-dimensional structure by comparative modeling

J Mol Graph Model. 1999 Apr;17(2):106-13, 134-6. doi: 10.1016/s1093-3263(99)00023-6.

Abstract

Whey acidic proteins (WAP) from the mouse, rat, rabbit, camel, and pig comprise two "four-disulfide core" domains. From a detailed analysis of all sequences containing this domain, we propose a new PROSITE motif ([KRHGVLN]-X-¿PF¿-X-[CF]-[PQSVLI]-X(9,19)-C-¿P¿-X-[DN]-X-¿N¿ -[CE]-X(5)-C-C) to accurately identify new four-disulfide 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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Camelus
  • Computer Simulation*
  • Disulfides / chemistry
  • Humans
  • Mice
  • Milk Proteins / chemistry*
  • Models, Molecular*
  • Molecular Sequence Data
  • Peptide Fragments / chemistry*
  • Peptide Library
  • Protein Conformation
  • Rabbits
  • Rats
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Swine
  • Whey Proteins

Substances

  • Disulfides
  • Milk Proteins
  • Peptide Fragments
  • Peptide Library
  • Whey Proteins