5U66
Modified single helix from the B-domain of protein A bound to IgG1 Fc
Summary for 5U66
| Entry DOI | 10.2210/pdb5u66/pdb |
| Related PRD ID | PRD_002261 |
| Descriptor | STAPLED PEPTIDE FROM DOMAIN B OF PROTEIN A, IgG1 fc derived from CD4-fc fusion, beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | igg1 fc, staple peptide, protein a, b-domain, immune system-inhibitor complex, immune system/inhibitor |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 26896.14 |
| Authors | Ultsch, M.H.,Eigenbrot, C. (deposition date: 2016-12-07, release date: 2017-05-24, Last modification date: 2023-11-15) |
| 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 (1.7 Å) |
Structure validation
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