ISSN:
1573-5001
Keywords:
S100B
;
Calcium-bound
;
Secondary structure
;
S100 protein family
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Abstract The NMR assignments of backbone 1H, 13C,and 15N resonances for calcium-bound human S100B werecompleted via heteronuclear multidimensional NMR spectroscopic techniques.NOE correlations, amide exchange, 3JHNHαcoupling constants, and CSI analysis were used to identify the secondarystructure for Ca-S100B. The protein is comprised of four helices (helix I,Glu2-;Arg20; helix II,Glu31-;Asn38; helix III,Gln50-;Thr59; helix IV,Phe70-;Phe87), three loops (loop I,Glu21-;His25; loop II,Glu39-;Glu49; loop III,Leu60-;Gly66), and two β-strands(strand I, Lys26〉-;Lys28; strand II,Glu67-;Asp69) which form a shortantiparallel β-sheet. Helix IV is extended by approximately one turnwhen compared to the secondary structures of apo-rat [Drohat et al. (1996)Biochemistry, 35, 11577-;11588] and bovine S100B [Kilby et al. (1996)Structure, 4, 1041-;1052]. In addition, several residues outside thecalcium-binding loops in S100B undergo significant backbone chemical shiftchanges upon binding calcium which are not observed in the related proteincalbindin D9k. Together these observations support previoussite-directed mutagenesis, absorption spectroscopy, and cysteine chemicalreactivity experiments, suggesting that the C-terminus in Ca-S100B isimportant for interactions with other proteins.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1018397213369
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