2l50 | pdb_00002l50

Solution structure of apo S100A16

spinqualitylabelsall models 2l50, 30 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2l50 is a 2 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 2l0u. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2l51 Gene: S100A16, S100F, AAG13 (Homo sapiens) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed The homodimeric structure of human S100A16 in the apo state has been obtained both in the solid state and in solution, resulting in good agreement between the structures with the exception of two loop regions. The homodimeric solution structure of human S100A16 was also calculated in the calcium(II)-bound form. Differently from most S100 proteins, the conformational rearrangement upon calcium binding is minor. This characteristic is likely to be related to the weak binding affinity of the protein for the calcium(II) ions. In turn, this is ascribed to the lack of the glutamate residue at the end of the S100-specific N-domain binding site, which in most S100 proteins provides two important side chain oxygen atoms as calcium(II) ligands. Furthermore, the presence of hydrophobic interactions stronger than for other S100 proteins, present in the closed form of S100A16 between the third and fourth helices, likely make the closed structure of the second EF-hand particularly stable, so even upon calcium(II) binding such a conformation is not disrupted. Structural characterization of human S100A16, a low-affinity calcium binder.,Babini E, Bertini I, Borsi V, Calderone V, Hu X, Luchinat C, Parigi G J Biol Inorg Chem. 2010 Nov 3. PMID:21046186 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also S100 protein

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