5U52
2 helix minimized version of the B-domain from Protein A (Z34C0 bound to IgG1 Fc (monoclinic form)
Summary for 5U52
Entry DOI | 10.2210/pdb5u52/pdb |
Related | 1L6X 5U4Y 5U66 |
Descriptor | IGG1 FC, Mini Z domain, beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
Functional Keywords | 2 helix bundle, protein a, b-domain, igg1 fc, immune system |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 4 |
Total formula weight | 58613.48 |
Authors | Ultsch, M.H.,Eigenbrot, C. (deposition date: 2016-12-06, release date: 2017-05-24, Last modification date: 2024-10-16) |
Primary citation | Ultsch, M.,Braisted, A.,Maun, H.R.,Eigenbrot, C. 3-2-1: Structural insights from stepwise shrinkage of a three-helix Fc-binding domain to a single helix. Protein Eng. Des. Sel., 30:619-625, 2017 Cited by PubMed Abstract: The well-studied B-domain from Staphylococcal protein A is a 59 amino acid three-helix bundle that binds the Fc portion of IgG with a dissociation constant of ~35 nM. The B-domain variant bearing a Gly to Ala mutation (=Z-domain) has been the subject of efforts to minimize a domain's size while retaining its function. We report X-ray crystallographic characterization of three steps in such a process using complexes with Fc: the full three-helix Z-domain, a 34 amino acid two-helix version called Z34C and a 13 amino acid single helix stabilized with an exo-helix tether, called LH1. PubMed: 28475752DOI: 10.1093/protein/gzx029 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.942 Å) |
Structure validation
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