2lt5

Publication Abstract from PubMed

Onconase((R)) FL-G zymogen is a 120 residue protein produced by circular permutation of the native Onconase((R)) sequence. In this construction, the wild type N- and C-termini are linked by a 16 residue segment and new N- and C-termini are generated at wild type positions R73 and S72. This novel segment linking the native N- and C-termini is designed to obstruct Onconase's((R)) active site and encloses a cleavage site for the HIV-1 protease. As a first step towards the resolution of its 3D structure and the study of its structure-function relationships, we report here the nearly complete NMR (1)H, (13)C and (15)N resonance chemical shift assignments at pH 5.2 and 35 degrees C (BMRB deposit no 17973). The results presented here clearly show that the structure of the wild type Onconase((R)) is conserved in the FL-G zymogen.

(1)H, (13)C and (15)N resonance assignments of the Onconase FL-G zymogen.,Serrano S, Callis M, Vilanova M, Benito A, Laurents DV, Ribo M, Bruix M Biomol NMR Assign. 2012 Mar 4. PMID:22392335^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.