AMINO-ACID-SEQUENCES OF OVOMUCOID 3RD DOMAINS FROM 27 ADDITIONAL SPECIES OF BIRDS

被引：36

作者：

APOSTOL, I ^{[1
]}

GILETTO, A ^{[1
]}

KOMIYAMA, T ^{[1
]}

ZHANG, WL ^{[1
]}

LASKOWSKI, M ^{[1
]}

机构：

[1] PURDUE UNIV, DEPT CHEM, W LAFAYETTE, IN 47907 USA

来源：

JOURNAL OF PROTEIN CHEMISTRY | 1993年 / 12卷 / 04期

关键词：

OVOMUCOID 3RD DOMAIN SEQUENCES; PROTEIN PROTEINASE INHIBITORS; EVOLUTION OF BIRDS;

D O I：

10.1007/BF01025042

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Ovomucoids consist of a single polypeptide chain which is composed of three tandem Kazal domains. Each Kazal domain is an actual or putative protein inhibitor of serine proteinases. Ovomucoid third domains were already isolated and sequenced from 126 species of birds (Laskowski et al., 1987, 1990). This paper adds 27 new species. A number of generalizations are made on the basis of sequences from 153 species. The residues that are in contact with the enzyme in enzyme-inhibitor complexes are strikingly hypervariable. While the primary specificity residue, P1, is the most variable; substitutions occur predominantly among aliphatic, hydrophobic residues. Consensus sequences for an avian ovomucoid third domain, for a b-type Kazal domain (i.e., a COOH terminal domain of multidomain inhibitors) and for a general Kazal domain are given. Finally, the individual new sequences are briefly discussed.

引用

页码：419 / 433

页数：15

共 44 条

[1] EFFECT OF SINGLE AMINO-ACID REPLACEMENTS ON THE THERMODYNAMICS OF THE REACTIVE SITE PEPTIDE-BOND HYDROLYSIS IN OVOMUCOID 3RD DOMAIN [J].