1q10

Ensemble of 40 Structures of the Dimeric Mutant of the B1 Domain of Streptococcal Protein G

spinqualitylabelsall models 1q10 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1q10 is a 2 chain structure with sequence from Streptococcus sp. 'group G'. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SPG1_STRSG Binds to the constant Fc region of IgG with high affinity. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Immunoglobulin-binding domain B1 of streptococcal protein G (GB1), a small (56 residues), stable, single-domain protein, is one of the most extensively used model systems in the area of protein folding and design. Recently, NMR and X-ray structures of a quintuple GB1 core mutant (L5V/A26F/F30V/Y33F/A34F) that showed an unexpected, intertwined tetrameric architecture were determined. Here, we report the NMR structure of another mutant, derived from the tetramer by reverting the single amino acid position F26 back to the wild-type sequence A26. The structure reveals a domain-swapped dimer that involves exchange of the second beta-hairpin. The resulting overall structure comprises an eight-stranded beta-sheet whose concave side is covered by two alpha helices. The dimer dissociates into a partially folded, monomeric species with a dissociation constant of 93(+/-10)microM. A protein contortionist: core mutations of GB1 that induce dimerization and domain swapping.,Byeon IJ, Louis JM, Gronenborn AM J Mol Biol. 2003 Oct 10;333(1):141-52. PMID:14516749 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Protein G

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