Crystal structure of the C-terminal Fg domain of human TNC with the mutations Y2140H and S2164H. Determined by X-ray diffraction at 1.8 Å resolution. Released 12 Jul 2023.
Explore 8FNB in 3D Show helices and sheets RCSB PDB PDBe
8FNB contains 24 α-helices and 32 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1984-1989 | 6 | |
| β-strand | 1996-2001 | 6 | 1 |
| α-helix | 2002-2004 | 3 | |
| α-helix | 2006-2008 | 3 | |
| β-strand | 2009-2015 | 7 | 1 |
| α-helix | 2018-2020 | 3 | |
| β-strand | 2023-2029 | 7 | 1 |
| α-helix | 2040-2045 | 6 | |
| β-strand | 2047-2048 | 2 | 1 |
| β-strand | 2054-2055 | 2 | 1 |
| α-helix | 2058-2065 | 8 | |
| β-strand | 2070-2078 | 9 | 1 |
| β-strand | 2081-2092 | 12 | 1 |
| α-helix | 2095-2097 | 3 | |
| β-strand | 2101-2108 | 8 | 1 |
| α-helix | 2115-2117 | 3 | |
| α-helix | 2120-2122 | 3 | |
| β-strand | 2123 | 1 | 2 |
| β-strand | 2124 | 1 | 3 |
| β-strand | 2127 | 1 | 3 |
| α-helix | 2136-2140 | 5 | |
| β-strand | 2144 | 1 | 2 |
| β-strand | 2152-2153 | 2 | 4 |
| β-strand | 2168-2169 | 2 | 4 |
| α-helix | 2170-2173 | 4 | |
| β-strand | 2181-2188 | 8 | 1 |
| α-helix | 2189-2193 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1984-1989 | 6 | |
| β-strand | 1996-2001 | 6 | 5 |
| α-helix | 2002-2004 | 3 | |
| α-helix | 2006-2008 | 3 | |
| β-strand | 2009-2015 | 7 | 5 |
| α-helix | 2018-2020 | 3 | |
| β-strand | 2023-2029 | 7 | 5 |
| α-helix | 2040-2045 | 6 | |
| β-strand | 2047-2048 | 2 | 5 |
| β-strand | 2054-2055 | 2 | 5 |
| α-helix | 2058-2065 | 8 | |
| β-strand | 2070-2078 | 9 | 5 |
| β-strand | 2081-2092 | 12 | 5 |
| α-helix | 2095-2097 | 3 | |
| β-strand | 2101-2108 | 8 | 5 |
| α-helix | 2115-2117 | 3 | |
| α-helix | 2120-2122 | 3 | |
| β-strand | 2123 | 1 | 6 |
| β-strand | 2124 | 1 | 7 |
| β-strand | 2127 | 1 | 7 |
| α-helix | 2136-2140 | 5 | |
| β-strand | 2144 | 1 | 6 |
| β-strand | 2152-2153 | 2 | 8 |
| β-strand | 2157 | 1 | 9 |
| β-strand | 2166 | 1 | 9 |
| β-strand | 2168-2169 | 2 | 8 |
| α-helix | 2170-2173 | 4 | |
| β-strand | 2181-2188 | 8 | 5 |
| α-helix | 2189-2193 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tenascin | A, B | protein | 231 | Homo sapiens | P24821 (AlphaFold model) |
>8FNB_1 Tenascin (chains A, B) GTGSGLLYPFPKDCSQAMLNGDTTSGLYTIYLNGDKAEALEVFCDMTSDGGGWIVFLRRK NGRENFYQNWKAYAAGFGDRREEFWLGLDNLNKITAQGQYELRVDLRDHGETAFAVYDKF SVGDAKTRYKLKVEGYSGTAGDSMAYHNGRSFSTFDKDTDSAITNCALSHKGAFWYRNCH RVNLMGRYGDNNHHQGVNWFHWKGHEHSIQFAEMKLRPSNFRNLEGRRKRA
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 2 |
Water and common crystallization additives (SO4) are not listed.
Protein-protein interactions between tenascin-R and RPTP zeta /phosphacan are critical to maintain the architecture of perineuronal nets. Sinha, A., Kawakami, J., Cole, K.S. et al. J Biol Chem (2023) 299:104952-104952. DOI 10.1016/j.jbc.2023.104952 · PubMed
Other PDB entries of the same protein (UniProt P24821 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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