1MWN

Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12

Summary for 1MWN

• Entry DOI: 10.2210/pdb1mwn/pdb
• Related: 1DT7
• NMR Information: BMRB: 5544
• Descriptor: S-100 protein, beta chain, F-actin capping protein alpha-1 subunit, CALCIUM ION (3 entities in total)
• Functional Keywords: s100b, trtk-12, calcium-binding, ef-hand, s100 protein, four helix bundle, helix loop helix, protein-peptide complex, 20 structures, structural protein
• Biological source: Rattus norvegicus (Norway rat); More
• Cellular location: Cytoplasm (By similarity): P04631; Cytoplasm, cytoskeleton (By similarity): P52907
• Total number of polymer chains: 4
• Total formula weight: 24631.86

Authors

Inman, K.G.,Yang, R.,Rustandi, R.R.,Miller, K.E.,Baldisseri, D.M.,Weber, D.J. (deposition date: 2002-09-30, release date: 2002-12-18, Last modification date: 2024-05-22)

Primary citation

Inman, K.G.,Yang, R.,Rustandi, R.R.,Miller, K.E.,Baldisseri, D.M.,Weber, D.J.
Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12
J.Mol.Biol., 324:1003-1014, 2002

PubMed Abstract: The solution NMR structure is reported for Ca(2+)-loaded S100B bound to a 12-residue peptide, TRTK-12, from the actin capping protein CapZ (alpha1 or alpha2 subunit, residues 265-276: TRTKIDWNKILS). This peptide was discovered by Dimlich and co-workers by screening a bacteriophage random peptide display library, and it matches exactly the consensus S100B binding sequence ((K/R)(L/I)XWXXIL). As with other S100B target proteins, a calcium-dependent conformational change in S100B is required for TRTK-12 binding. The TRTK-12 peptide is an amphipathic helix (residues W7 to S12) in the S100B-TRTK complex, and helix 4 of S100B is extended by three or four residues upon peptide binding. However, helical TRTK-12 in the S100B-peptide complex is uniquely oriented when compared to the three-dimensional structures of other S100-peptide complexes. The three-dimensional structure of the S100B-TRTK peptide complex illustrates that residues in the S100B binding consensus sequence (K4, I5, W7, I10, L11) are all involved in the S100B-peptide interface, which can explain its orientation in the S100B binding pocket and its relatively high binding affinity. A comparison of the S100B-TRTK peptide structure to the structures of apo- and Ca(2+)-bound S100B illustrates that the binding site of TRTK-12 is buried in apo-S100B, but is exposed in Ca(2+)-bound S100B as necessary to bind the TRTK-12 peptide.

PubMed: 12470955
DOI: 10.1016/S0022-2836(02)01152-X

Experimental method

SOLUTION NMR