4WQQ

Structure of EPNH mutant of CEL-I

Summary for 4WQQ

• Entry DOI: 10.2210/pdb4wqq/pdb
• Descriptor: Lectin CEL-I, N-acetyl-D-galactosamine-specific C-type, CALCIUM ION, alpha-D-mannopyranose, ... (4 entities in total)
• Functional Keywords: cel-i, epnh munant, c-type lectin, mannose recognition, sugar binding protein
• Biological source: Cucumaria echinata (Sea cucumber)
• Total number of polymer chains: 4
• Total formula weight: 65719.14

Authors

Unno, H.,Hatakeyama, T. (deposition date: 2014-10-22, release date: 2015-04-29, Last modification date: 2024-11-06)

Primary citation

Moriuchi, H.,Unno, H.,Goda, S.,Tateno, H.,Hirabayashi, J.,Hatakeyama, T.
Mannose-recognition mutant of the galactose/N-acetylgalactosamine-specific C-type lectin CEL-I engineered by site-directed mutagenesis.
Biochim.Biophys.Acta, 1850:1457-1465, 2015

PubMed Abstract: CEL-I is a galactose/N-acetylgalactosamine-specific C-type lectin isolated from the sea cucumber Cucumaria echinata. Its carbohydrate-binding site contains a QPD (Gln-Pro-Asp) motif, which is generally recognized as the galactose specificity-determining motif in the C-type lectins. In our previous study, replacement of the QPD motif by an EPN (Glu-Pro-Asn) motif led to a weak binding affinity for mannose. Therefore, we examined the effects of an additional mutation in the carbohydrate-binding site on the specificity of the lectin.

PubMed: 25869490
DOI: 10.1016/j.bbagen.2015.04.004

Experimental method

X-RAY DIFFRACTION (1.7 Å)