The use of dipolar couplings for determining the solution structure of rat apo-S100B(betabeta).

Printer-friendly versionPrinter-friendly versionPDF versionPDF version
TitleThe use of dipolar couplings for determining the solution structure of rat apo-S100B(betabeta).
Publication TypeJournal Article
Year of Publication1999
AuthorsDrohat, AC, Tjandra, N, Baldisseri, DM, Weber, DJ
JournalProtein Sci
Volume8
Issue4
Pagination800-9
Date Published1999 Apr
ISSN0961-8368
KeywordsAnimals, Calcium-Binding Proteins, Magnetic Resonance Spectroscopy, Models, Molecular, Nerve Growth Factors, Protein Structure, Secondary, Rats, S100 Proteins, Sequence Homology, Amino Acid, Statistics as Topic
Abstract

The relative orientations of adjacent structural elements without many well-defined NOE contacts between them are typically poorly defined in NMR structures. For apo-S100B(betabeta) and the structurally homologous protein calcyclin, the solution structures determined by conventional NMR exhibited considerable differences and made it impossible to draw unambiguous conclusions regarding the Ca2+-induced conformational change required for target protein binding. The structure of rat apo-S100B(betabeta) was recalculated using a large number of constraints derived from dipolar couplings that were measured in a dilute liquid crystalline phase. The dipolar couplings orient bond vectors relative to a single-axis system, and thereby remove much of the uncertainty in NOE-based structures. The structure of apo-S100B(betabeta) indicates a minimal change in the first, pseudo-EF-hand Ca2+ binding site, but a large reorientation of helix 3 in the second, classical EF-hand upon Ca2+ binding.

DOI10.1110/ps.8.4.800
Alternate JournalProtein Sci.
PubMed ID10211826
PubMed Central IDPMC2144316
Grant ListR01GM58888 / GM / NIGMS NIH HHS / United States
S10RR10441 / RR / NCRR NIH HHS / United States