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

被引：128

作者：

Ranganathan, S

Simpson, KJ

Shaw, DC

Nicholas, KR

机构：

[1] Univ Sydney, Australian Genom Informat Ctr, Sydney, NSW 2006, Australia

[2] Victorian Inst Anim Sci, Attwood, Vic, Australia

[3] La Trobe Univ, Sch Agr Sci, Bundoora, Vic 3083, Australia

[4] Australian Natl Univ, John Curtin Sch Med Res, Prot Biochem Grp, Canberra, ACT 2601, Australia

来源：

JOURNAL OF MOLECULAR GRAPHICS & MODELLING | 1999年 / 17卷 / 02期

基金：

澳大利亚研究理事会;

关键词：

WAP; molecular model; sequence motifs; sequence-structure comparison; molecular electrostatic potential; four-disulfide core;

D O I：

10.1016/S1093-3263(99)00023-6

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 model for the WAP proteins is proposed, bread on the human mucous proteinase inhibitor crystal structure. This article presents a detailed atomic model for the two-domain porcine WAP sequence by comparitive modeling. Surface electrostatic potential calculation 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. (C) 2000 by Elsevier Science Inc.

引用

页码：106 / +

页数：11

共 34 条

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