5EYX
Monoclinic Form of Centrolobium tomentosum seed lectin (CTL) complexed with Man1-3Man-OMe.
Summary for 5EYX
| Entry DOI | 10.2210/pdb5eyx/pdb |
| Related | 5EYY |
| Descriptor | Centrolobium tomentosum lectin, alpha-D-mannopyranose-(1-3)-methyl alpha-D-mannopyranoside, CALCIUM ION, ... (6 entities in total) |
| Functional Keywords | lectin, centrolobium tomentosum, dalbergieae, methyl dimannoside, ctl, sugar binding protein |
| Biological source | Centrolobium tomentosum |
| Total number of polymer chains | 2 |
| Total formula weight | 55508.72 |
| Authors | Almeida, A.C.,Osterne, V.J.S.,Santiago, M.Q.,Pinto-Junior, V.R.,Silva-Filho, J.C.,Lossio, C.F.,Almeida, R.P.H.,Teixeira, C.S.,Delatorre, P.,Rocha, B.A.M.,Santiago, K.S.,Cavada, B.S. (deposition date: 2015-11-25, release date: 2016-03-16, Last modification date: 2024-10-23) |
| Primary citation | Almeida, A.C.,Osterne, V.J.,Santiago, M.Q.,Pinto-Junior, V.R.,Silva-Filho, J.C.,Lossio, C.F.,Nascimento, F.L.,Almeida, R.P.,Teixeira, C.S.,Leal, R.B.,Delatorre, P.,Rocha, B.A.,Assreuy, A.M.,Nascimento, K.S.,Cavada, B.S. Structural analysis of Centrolobium tomentosum seed lectin with inflammatory activity. Arch.Biochem.Biophys., 596:73-83, 2016 Cited by PubMed Abstract: A glycosylated lectin (CTL) with specificity for mannose and glucose has been detected and purified from seeds of Centrolobium tomentosum, a legume plant from Dalbergieae tribe. It was isolated by mannose-sepharose affinity chromatography. The primary structure was determined by tandem mass spectrometry and consists of 245 amino acids, similar to other Dalbergieae lectins. CTL structures were solved from two crystal forms, a monoclinic and a tetragonal, diffracted at 2.25 and 1.9 Å, respectively. The carbohydrate recognition domain (CRD), metal-binding site and glycosylation site were characterized, and the structural basis for mannose/glucose-binding was elucidated. The lectin adopts the canonical dimeric organization of legume lectins. CTL showed acute inflammatory effect in paw edema model. The protein was subjected to ligand screening (dimannosides and trimannoside) by molecular docking, and interactions were compared with similar lectins possessing the same ligand specificity. This is the first crystal structure of mannose/glucose native seed lectin with proinflammatory activity isolated from the Centrolobium genus. PubMed: 26946944DOI: 10.1016/j.abb.2016.03.001 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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