2JDM
Mutant (S22A) of Pseudomonas aeruginosa lectin II (PA-IIL) complexed with methyl-a-L-fucopyranoside
Summary for 2JDM
Entry DOI | 10.2210/pdb2jdm/pdb |
Related | 1GZT 1OUR 1OUS 1OUX 1OVP 1OVS 1OXC 1UZV 1W43 1W8F 1W8H 2BOJ 2BP6 2JDH 2JDK 2JDN 2JDP |
Descriptor | FUCOSE-BINDING LECTIN PA-IIL, CALCIUM ION, SULFATE ION, ... (6 entities in total) |
Functional Keywords | ectin, glycomimetic, cystic fibrosis, lectin |
Biological source | PSEUDOMONAS AERUGINOSA |
Total number of polymer chains | 4 |
Total formula weight | 48611.07 |
Authors | Adam, J.,Pokorna, M.,Sabin, C.,Mitchell, E.P.,Imberty, A.,Wimmerova, M. (deposition date: 2007-01-11, release date: 2007-06-12, Last modification date: 2023-12-13) |
Primary citation | Adam, J.,Pokorna, M.,Sabin, C.,Mitchell, E.P.,Imberty, A.,Wimmerova, M. Engineering of Pa-Iil Lectin from Pseudomonas Aeruginosa - Unravelling the Role of the Specificity Loop for Sugar Preference. Bmc Struct.Biol., 7:36-, 2007 Cited by PubMed Abstract: Lectins are proteins of non-immune origin capable of binding saccharide structures with high specificity and affinity. Considering the high encoding capacity of oligosaccharides, this makes lectins important for adhesion and recognition. The present study is devoted to the PA-IIL lectin from Pseudomonas aeruginosa, an opportunistic human pathogen capable of causing lethal complications in cystic fibrosis patients. The lectin may play an important role in the process of virulence, recognizing specific saccharide structures and subsequently allowing the bacteria to adhere to the host cells. It displays high values of affinity towards monosaccharides, especially fucose--a feature caused by unusual binding mode, where two calcium ions participate in the interaction with saccharide. Investigating and understanding the nature of lectin-saccharide interactions holds a great potential of use in the field of drug design, namely the targeting and delivery of active compounds to the proper site of action. PubMed: 17540045DOI: 10.1186/1472-6807-7-36 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
Download full validation report