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 language | English |
|---|---|
| Pages (from-to) | 106-113 |
| Number of pages | 8 |
| Journal | Journal of Molecular Graphics and Modelling |
| Volume | 17 |
| Issue number | 2 |
| Publication status | Published - Apr 1999 |
| Externally published | Yes |
Keywords
- Four-disitlflde core
- Molecular electrostatic potential
- Molecular model
- Sequence motifs
- Sequence-structure comparison
- WAP
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