Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy

Kristen M. Vallely, Richard R. Rustandi, Karen C. Ellis, Olga Varlamova, Anne R. Bresnick, David J. Weber

Research output: Contribution to journalArticle

61 Citations (Scopus)

Abstract

Mts1 is a member of the S100 family of Ca2+-binding proteins and is implicated in promoting tumor progression and metastasis. To better understand the structure-function relationships of this protein and to begin characterizing its Ca2+-dependent interaction with protein binding targets, the three-dimensional structure of mts1 was determined in the apo state by NMR spectroscopy. As with other S100 protein family members, mts1 is a symmetric homodimer held together by noncovalent interactions between two helices from each subunit (helices 1, 4, 1′, and 4′) to form an X-type four-helix bundle. Each subunit of mts1 has two EF-hand Ca2+-binding domains: a pseudo-EF-hand (or S100-hand) and a typical EF-hand that are brought into proximity by a small two-stranded antiparallel β-sheet. The S100-hand is formed by helices 1 and 2, and is similar in conformation to other members of the S100 family. In the typical EF-hand, the position of helix 3 is similar to that of another member of the S100 protein family, calcyclin (S100A6), and less like that of other S100 family members for which three-dimensional structures are available in the calcium-free state (e.g., S100B and S100A1). The differences in the position of helix 3 in the apo state of these four S100 proteins are likely due to variations in the amino acid sequence in the C-terminus of helix 4 and in loop 2 (the hinge region) and could potentially be used to subclassify the S100 protein family.

Original languageEnglish (US)
Pages (from-to)12670-12680
Number of pages11
JournalBiochemistry
Volume41
Issue number42
DOIs
StatePublished - Oct 22 2002

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EF Hand Motifs
S100 Proteins
Nuclear magnetic resonance spectroscopy
Magnetic Resonance Spectroscopy
Hand
Hinges
Protein Binding
Conformations
Tumors
Amino Acid Sequence
Carrier Proteins
Neoplasm Metastasis
Calcium
Amino Acids
Neoplasms
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Vallely, K. M., Rustandi, R. R., Ellis, K. C., Varlamova, O., Bresnick, A. R., & Weber, D. J. (2002). Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy. Biochemistry, 41(42), 12670-12680. https://doi.org/10.1021/bi020365r

Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy. / Vallely, Kristen M.; Rustandi, Richard R.; Ellis, Karen C.; Varlamova, Olga; Bresnick, Anne R.; Weber, David J.

In: Biochemistry, Vol. 41, No. 42, 22.10.2002, p. 12670-12680.

Research output: Contribution to journalArticle

Vallely, KM, Rustandi, RR, Ellis, KC, Varlamova, O, Bresnick, AR & Weber, DJ 2002, 'Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy', Biochemistry, vol. 41, no. 42, pp. 12670-12680. https://doi.org/10.1021/bi020365r
Vallely KM, Rustandi RR, Ellis KC, Varlamova O, Bresnick AR, Weber DJ. Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy. Biochemistry. 2002 Oct 22;41(42):12670-12680. https://doi.org/10.1021/bi020365r
Vallely, Kristen M. ; Rustandi, Richard R. ; Ellis, Karen C. ; Varlamova, Olga ; Bresnick, Anne R. ; Weber, David J. / Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy. In: Biochemistry. 2002 ; Vol. 41, No. 42. pp. 12670-12680.
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