Nuclear magnetic resonance assignments and secondary structure of bovine S100 beta protein.

Abstract:

:S100 beta is a neurite extension factor and has been implicated in Alzheimer's disease and Down's syndrome. It belongs to a group of low molecular weight calcium-binding proteins containing the helix-loop-helix calcium binding motif. The structure of only one S100 protein, calbindin D9k, which has the lowest sequence similarity to the other members of the S100 group has been determined. We report the NMR assignments and secondary structure of calcium-free S100 beta. The secondary structure is similar to that of calbindin D9k, determined using NMR, except that there is clear evidence for an additional well ordered 5-residue alpha-helix in S100 beta.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Kilby PM,Van Eldik LJ,Roberts GC

doi

10.1016/0014-5793(95)00296-l

subject

Has Abstract

pub_date

1995-04-17 00:00:00

pages

90-6

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(95)00296-L

journal_volume

363

pub_type

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