7CYA
Saimiri boliviensis boliviensis galectin-13 with lactose
Summary for 7CYA
| Entry DOI | 10.2210/pdb7cya/pdb |
| Related PRD ID | PRD_900004 |
| Descriptor | Galectin, beta-D-galactopyranose-(1-4)-beta-D-glucopyranose (3 entities in total) |
| Functional Keywords | saimiri boliviensis boliviensis galectin-13 with lactose, sugar binding protein |
| Biological source | Saimiri boliviensis boliviensis (Bolivian squirrel monkey) |
| Total number of polymer chains | 1 |
| Total formula weight | 16831.09 |
| Authors | |
| Primary citation | Li, X.,Yao, Y.,Liu, T.,Gu, K.,Han, Q.,Zhang, W.,Ayala, G.J.,Liu, Y.,Na, H.,Yu, J.,Zhang, F.,Mayo, K.H.,Su, J. Actin binding to galectin-13/placental protein-13 occurs independently of the galectin canonical ligand-binding site. Glycobiology, 31:1219-1229, 2021 Cited by PubMed Abstract: The gene for galectin-13 (Gal-13, placental protein 13) is only present in primates, and its low expression level in maternal serum may promote preeclampsia. In the present study, we used pull-down experiments and biolayer interferometry to assess the interaction between Gal-13 and actin. These studies uncovered that human Gal-13 (hGal-13) and Saimiri boliviensis boliviensis (sGal-13) strongly bind to α- and β-/γ-actin, with Ca2+ and adenosine triphosphate, significantly enhancing the interactions. This in turn suggests that h/sGal-13 may inhibit myosin-induced contraction when vascular smooth muscle cells undergo polarization. Here, we solved the crystal structure of sGal-13 bound to lactose and found that it exists as a monomer in contrast to hGal-13 which is a dimer. The distribution of sGal-13 in HeLa cells is similar to that of hGal-13, indicating that monomeric Gal-13 is the primary form in cells. Even though sGal-13 binds to actin, hGal-13 ligand-binding site mutants do not influence hGal-13/actin binding, whereas the monomeric mutant C136S/C138S binds to actin more strongly than the wild-type hGal-13. Overall, our study demonstrates that monomeric Gal-13 binds to actin, an interaction that is independent of the galectin canonical ligand-binding site. PubMed: 34080003DOI: 10.1093/glycob/cwab047 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.71 Å) |
Structure validation
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