6I9Q
Structure of the mouse CD98 heavy chain ectodomain
Summary for 6I9Q
| Entry DOI | 10.2210/pdb6i9q/pdb |
| Descriptor | 4F2 cell-surface antigen heavy chain, 1,2-ETHANEDIOL, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | cd98hc, 4f2hc, amino acid transport, cd98 light chain, lat-1, lat-2, integrin beta subunit binding, single-pass type ii membrane protein, membrane protein |
| Biological source | Mus musculus (Mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 48526.16 |
| Authors | Schiefner, A.,Deuschle, F.-C.,Skerra, A. (deposition date: 2018-11-24, release date: 2019-04-17, Last modification date: 2024-01-24) |
| Primary citation | Deuschle, F.C.,Schiefner, A.,Skerra, A. Structural differences between the ectodomains of murine and human CD98hc. Proteins, 87:693-698, 2019 Cited by PubMed Abstract: The CD98 heavy chain (CD98hc) constitutes both a promising cell surface target for the treatment of cancers and a transcytosis receptor potentially useful for the brain delivery of therapeutics. However, pharmacokinetic studies and safety assessment of cognate antibodies or nonimmunoglobulin binding proteins in rodents is hampered by cross-species variability of both amino acid sequence and glycosylation pattern. Here, we report the crystal structure of the murine CD98hc extracellular domain and a comprehensive comparison with its human ortholog, revealing only one conserved surface patch that is neither shielded by glycosylation nor by the cell membrane with an accessible surface area typical for an antibody epitope. Our results imply the necessity of a surrogate approach for CD98hc-specific binding proteins with predictive power for clinical investigations. PubMed: 30958588DOI: 10.1002/prot.25686 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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