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2YMZ

Crystal structure of chicken Galectin 2

Summary for 2YMZ
Entry DOI10.2210/pdb2ymz/pdb
Related PRD IDPRD_900004
DescriptorGALECTIN 2, beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, SULFATE ION, ... (4 entities in total)
Functional Keywordssugar binding protein, carbohydrate recognition
Biological sourceGALLUS GALLUS (CHICKEN)
Total number of polymer chains6
Total formula weight90864.88
Authors
Fernandez, I.S.,Ruiz, F.M.,Solis, D.,Gabius, H.-J.,Romero, A. (deposition date: 2012-10-11, release date: 2013-08-28, Last modification date: 2023-12-20)
Primary citationRuiz, F.M.,Fernandez, I.S.,Lopez-Merino, L.,Lagartera, L.,Kaltner, H.,Menendez, M.,Andre, S.,Solis, D.,Gabius, H.-J.,Romero, A.
Fine-Tuning of Prototype Chicken Galectins: Structure of Cg-2 and Structure-Activity Correlations
Acta Crystallogr.,Sect.D, 69:1665-, 2013
Cited by
PubMed Abstract: The comparatively small number of members of the family of adhesion/growth-regulatory galectins in chicken predestines this system as an attractive model to study the divergence of these lectins after gene duplication. Expression profiling of the three homodimeric (prototype) chicken galectins (CG-1A, CG-1B and CG-2) has raised evidence of distinct functionalities, explaining the interest in a detailed crystallographic analysis of CG-2. As revealed here, marked differences are found in the ligand-binding site and in the contact pattern within the homodimer interface, underlying a characteristic orientation of the two subunits. Notably, a distinctive trimer of dimers that is unique in all galectin crystal structures reported to date forms the core unit of the crystallographic assembly. Combination with spectroscopic and thermodynamic measurements, and comparisons with CG-1A and CG-1B, identify differential changes in the circular-dichroism spectra in the presence of lactose, reflecting the far-reaching impact of the ligand on hydrodynamic behaviour, and inter-galectin differences in both the entropy and the enthalpy of binding. This structural information is a salient step to complete the analysis of the full set of galectins from this model organism.
PubMed: 23999290
DOI: 10.1107/S0907444913011773
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.75 Å)
Structure validation

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数据于2025-07-30公开中

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