4XZP

Crystal structure of the N-terminal domain of human galectin-4

Summary for 4XZP

• Entry DOI: 10.2210/pdb4xzp/pdb
• Related: 5CBL
• Descriptor: Galectin-4, CALCIUM ION (3 entities in total)
• Functional Keywords: galectins, beta-galactosides binding, sugar binding protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 19346.95

Authors

Rustiguel, J.K.,Nonato, M.C. (deposition date: 2015-02-04, release date: 2016-03-02, Last modification date: 2023-09-27)

Primary citation

Rustiguel, J.K.,Soares, R.O.,Meisburger, S.P.,Davis, K.M.,Malzbender, K.L.,Ando, N.,Dias-Baruffi, M.,Nonato, M.C.
Full-length model of the human galectin-4 and insights into dynamics of inter-domain communication.
Sci Rep, 6:33633-33633, 2016

PubMed Abstract: Galectins are proteins involved in diverse cellular contexts due to their capacity to decipher and respond to the information encoded by β-galactoside sugars. In particular, human galectin-4, normally expressed in the healthy gastrointestinal tract, displays differential expression in cancerous tissues and is considered a potential drug target for liver and lung cancer. Galectin-4 is a tandem-repeat galectin characterized by two carbohydrate recognition domains connected by a linker-peptide. Despite their relevance to cell function and pathogenesis, structural characterization of full-length tandem-repeat galectins has remained elusive. Here, we investigate galectin-4 using X-ray crystallography, small- and wide-angle X-ray scattering, molecular modelling, molecular dynamics simulations, and differential scanning fluorimetry assays and describe for the first time a structural model for human galectin-4. Our results provide insight into the structural role of the linker-peptide and shed light on the dynamic characteristics of the mechanism of carbohydrate recognition among tandem-repeat galectins.

PubMed: 27642006
DOI: 10.1038/srep33633

Experimental method

X-RAY DIFFRACTION (1.48 Å)