Sequential 1H NMR Assignments and Secondary Structure of Aponeocarzinostatin in Solution

M. Lyndsay Remerowski, Steffen J. Glaser, Gary P. Drobny, Larry C. Sieker, T. S.Anantha Samy

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23 Scopus citations

Abstract

Sequential assignments and secondary structural analysis have been accomplished for the 113-residue apoprotein of the antitumor drug neocarzinostatin (NCS) from Streptomyces carzinostaticus. A total of 98% of the main-chain and 77% of the side-chain resonances have been sequence specifically assigned by use of information from coherence transfer experiments and by sequential and interstrand NOEs. Because of the complexity of the NCS spectrum, several sequential assignment strategies were employed to complete the analysis. Apo-NCS consists of three antiparallel β-sheeted domains by NMR analysis. There is an extensive four-strand antiparallel β-sheet, and two two-stranded domains. One of the two-strand domains is contiguous, S72–N87, with chain reversal occurring through the region L77–R82. The other two-stranded domain has the section G16–A24 antiparallel with respect to the region S62-R70. This secondary structure is consistent with the crystal structure of holo-NCS at 2.8-Å resolution.

Original languageEnglish
Pages (from-to)8401-8409
Number of pages9
JournalBiochemistry
Volume29
Issue number36
DOIs
StatePublished - 1 Sep 1990
Externally publishedYes

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