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

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Date

1999

Authors

Ranganathan, Shoba
Simpson, Kaylene
Shaw, Denis
Nicholas, K R

Journal Title

Journal ISSN

Volume Title

Publisher

Elsevier

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.

Description

Keywords

Keywords: disulfide; milk protein; peptide fragment; peptide library; whey protein; amino acid sequence; animal; article; camel; chemical structure; chemistry; comparative study; computer simulation; human; molecular genetics; mouse; protein conformation; rabbit; r Four-disitlflde core; Molecular electrostatic potential; Molecular model; Sequence motifs; Sequence-structure comparison; WAP

Citation

URI

http://hdl.handle.net/1885/92465

Collections

ANU Research Publications

Source

Journal of Molecular Graphics and Modelling

Type

Journal article

Book Title

Entity type

Access Statement

License Rights

DOI

Restricted until

2037-12-31

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