6A9Y
The crystal structure of Mu homology domain of SGIP1
Summary for 6A9Y
| Entry DOI | 10.2210/pdb6a9y/pdb |
| Descriptor | SH3-containing GRB2-like protein 3-interacting protein 1 (2 entities in total) |
| Functional Keywords | sgip1, dimer, disulfide bond, endocytosis |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 31269.52 |
| Authors | |
| Primary citation | Zhang, Y.,Feng, Y.,Xin, Y.,Liu, X. SGIP1 dimerizes via intermolecular disulfide bond in mu HD domain during cellular endocytosis. Biochem. Biophys. Res. Commun., 505:99-105, 2018 Cited by PubMed Abstract: Along with its homologs FCHo1 and FCHo2, SGIP1 plays an important role in clathrin-mediated endocytosis. The highly conserved C-terminal μHD domains in these proteins are the critical regions interacting with adapter molecules such as Eps15. The crystal structure of μHD domain of SGIP1 has been reported previously. In this study, we found that μHD domain of SGIP1 is capable of forming a stable dimer by an intermolecular disulfide bond formed by C632 in our crystal structure. The mutational study of C632 revealed that this residue is important for the function of SGIP1 during cellular endocytosis. Our study revealed a new dimerization and/or oligomerization manner in theses adaptor proteins, which is a critical prerequisite for their proper function. PubMed: 30236986DOI: 10.1016/j.bbrc.2018.09.075 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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