Format

Send to

Choose Destination
See comment in PubMed Commons below
Biochemistry. 1998 Apr 7;37(14):4712-21.

The solution structure of type II antifreeze protein reveals a new member of the lectin family.

Author information

1
Protein Engineering Network of Centres of Excellence, University of Alberta, Edmonton, Alberta T6G 2S2, Canada.

Abstract

A recombinant form of the sea raven type II antifreeze protein (SRAFP) has been produced using the Pichia pastoris expression system. The antifreeze activity of recombinant SRAFP is indistinguishable from that of the wild-type protein. The global fold of SRAFP has been determined by two-dimensional 1H homonuclear and three-dimensional 1H-¿15N¿ heteronuclear NMR spectroscopy using 785 NOE distance restraints and 47 angular restraints. The molecule folds into one globular domain that consists of two helices and nine beta-strands in two beta-sheets. The structure confirms the proposed existence of five disulfide bonds. The global fold of SRAFP is homologous to C-type lectins and pancreatic stone proteins, even though the sequence identity is only approximately 20%.

PMID:
9537986
DOI:
10.1021/bi972788c
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for American Chemical Society
    Loading ...
    Support Center