This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1b4c
From Proteopedia
|
SOLUTION STRUCTURE OF RAT APO-S100B USING DIPOLAR COUPLINGS
Overview
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.
About this Structure
1B4C is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
The use of dipolar couplings for determining the solution structure of rat apo-S100B(betabeta)., Drohat AC, Tjandra N, Baldisseri DM, Weber DJ, Protein Sci. 1999 Apr;8(4):800-9. PMID:10211826
Page seeded by OCA on Tue Nov 20 11:20:59 2007
