1m31
From Proteopedia
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Three-Dimensional Solution Structure of Apo-Mts1
Overview
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 beta-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.
About this Structure
1M31 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy., Vallely KM, Rustandi RR, Ellis KC, Varlamova O, Bresnick AR, Weber DJ, Biochemistry. 2002 Oct 22;41(42):12670-80. PMID:12379109
Page seeded by OCA on Mon Nov 12 18:06:34 2007
