A small trypsin inhibitor from the frog of Odorrana grahami.
A novel peptide inhibitor (OGTI) of serine protease with a molecular weight of 1949.8, was purified from the skin secretion of the frog, Odorrana grahami. Of the tested serine proteases, OGTI only inhibited the hydrolysis activity of trypsin on synthetic chromogenic substrate. This precursor deduced from the cDNA sequence is composed of 70 amino acid residues. The mature OGTI contains 17 amino acid residues including a six-residue loop disulfided by two half-cysteines (AVNIPFKVHFRCKAAFC). In addition to its unique six-residue loop, the overall structure and precursor of OGTI are different from those of other serine protease inhibitors. It is also one of the smallest serine protease inhibitors ever found.
Li
Jianxu
J
Biotoxin Units of Key Laboratory of Animal Models and Human Disease Mechanisms, Kunming Institute of Zoology, Chinese Academy of Sciences (CAS), Kunming 650223, Yunnan, China.
Wu
Jing
J
Wang
Yipeng
Y
Xu
Xueqing
X
Liu
Tongguang
T
Lai
Ren
R
Zhu
Huajie
H
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D017124:Conserved Sequence; D005260:Female; D008297:Male; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D011898:Ranidae; D016415:Sequence Alignment; D014357:Trypsin / Q000378:metabolism; D014361:Trypsin Inhibitors / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification* / Q000494:pharmacology
D014361:Trypsin Inhibitors; D014357:Trypsin