2CE6
Structure of Helix Pomatia agglutinin with no ligands
Summary for 2CE6
| Entry DOI | 10.2210/pdb2ce6/pdb |
| Related | 2CCV |
| Descriptor | HELIX POMATIA AGGLUTININ (2 entities in total) |
| Functional Keywords | lectin, snail, helix pomatia |
| Biological source | HELIX POMATIA (ROMAN SNAIL) |
| Total number of polymer chains | 1 |
| Total formula weight | 11338.78 |
| Authors | Sanchez, J.-F.,Lescar, J.,Chazalet, V.,Audfray, A.,Gautier, C.,Gagnon, J.,Breton, C.,Imberty, A.,Mitchell, E.P. (deposition date: 2006-02-03, release date: 2006-05-15, Last modification date: 2024-11-06) |
| Primary citation | Sanchez, J.-F.,Lescar, J.,Chazalet, V.,Audfray, A.,Gagnon, J.,Alvarez, R.,Breton, C.,Imberty, A.,Mitchell, E.P. Biochemical and Structural Analysis of Helix Pomatia Agglutinin. A Hexameric Lectin with a Novel Fold. J.Biol.Chem., 281:20171-, 2006 Cited by PubMed Abstract: Helix pomatia agglutinin (HPA) is a N-acetylgalactosamine (GalNAc) binding lectin found in the albumen gland of the roman snail. As a constituent of perivitelline fluid, HPA protects fertilized eggs from bacteria and is part of the innate immunity system of the snail. The peptide sequence deduced from gene cloning demonstrates that HPA belongs to a family of carbohydrate-binding proteins recently identified in several invertebrates. This domain is also present in discoidin from the slime mold Dictyostelium discoideum. Investigation of the lectin specificity was performed with the use of glycan arrays, demonstrating that several GalNAc-containing oligosaccharides are bound and rationalizing the use of this lectin as a cancer marker. Titration microcalorimetry performed on the interaction between HPA and GalNAc indicates an affinity in the 10(-4) M range with an enthalpy-driven binding mechanism. The crystal structure of HPA demonstrates the occurrence of a new beta-sandwich lectin fold. The hexameric quaternary state was never observed previously for a lectin. The high resolution structure complex of HPA with GalNAc characterizes a new carbohydrate binding site and rationalizes the observed preference for alphaGalNAc-containing oligosaccharides. PubMed: 16704980DOI: 10.1074/JBC.M603452200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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