5CBL
Crystal structure of the C-terminal domain of human galectin-4 with lactose
Summary for 5CBL
| Entry DOI | 10.2210/pdb5cbl/pdb |
| Related | 4XZP |
| Related PRD ID | PRD_900004 |
| Descriptor | Galectin-4, beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, BETA-MERCAPTOETHANOL, ... (6 entities in total) |
| Functional Keywords | galectins, beta-galactosides binding, sugar binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 4 |
| Total formula weight | 67230.06 |
| Authors | Rustiguel, J.K.,Nonato, M.C. (deposition date: 2015-07-01, release date: 2015-11-04, Last modification date: 2024-05-01) |
| Primary citation | Rustiguel, J.K.,Kumagai, P.S.,Dias-Baruffi, M.,Costa-Filho, A.J.,Nonato, M.C. Recombinant expression, purification and preliminary biophysical and structural studies of C-terminal carbohydrate recognition domain from human galectin-4. Protein Expr.Purif., 118:39-48, 2015 Cited by PubMed Abstract: Galectin-4 (Gal4), a tandem-repeat type galectin, is expressed in healthy epithelium of the gastrointestinal tract. Altered levels of Gal4 expression are associated with different types of cancer, suggesting its usage as a diagnostic marker as well as target for drug development. The functional data available for this class of proteins suggest that the wide spectrum of cellular activities reported for Gal4 relies on distinct glycan specificity and structural characteristics of its two carbohydrate recognition domains. In the present work, two independent constructs for recombinant expression of the C-terminal domain of human galectin-4 (hGal4-CRD2) were developed. His6-tagged and untagged recombinant proteins were overexpressed in Escherichia coli, and purified by affinity chromatography followed by gel filtration. Correct folding and activity of hGal4-CRD2 were assessed by circular dichroism and fluorescence spectroscopies, respectively. Diffraction quality crystals were obtained by vapor-diffusion sitting drop setup and the crystal structure of CRD2 was solved by molecular replacement techniques at 1.78 Å resolution. Our work describes the development of important experimental tools that will allow further studies in order to correlate structure and binding properties of hGal4-CRD2 and human galectin-4 functional activities. PubMed: 26432949DOI: 10.1016/j.pep.2015.09.026 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.781 Å) |
Structure validation
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