Protein Family Models

This entry primarily matches to legume-like lectin domains found in prokaryotes. (from Pfam)

Date:

2024-11-04

Ths presumed domain is found in the CshA protein from Streptococcus gordonii. The domain is named after the sequence found in CshA in the conserved C-terminal region. The conserved negatively charged residues suggests that this domain may bind to calcium ions. This domain is part of the non-repetitive region NR3 [1]. [1]. 27920201. The Streptococcus gordonii Adhesin CshA Protein Binds Host Fibronectin via a Catch-Clamp Mechanism. Back CR, Sztukowska MN, Till M, Lamont RJ, Jenkinson HF, Nobbs AH, Race PR;. J Biol Chem. 2017;292:1538-1549. (from Pfam)

Date:

2024-10-16

The multifunctional fibrillar adhesin CshA, which mediates binding to both host molecules and other microorganisms, is an important determinant of colonization by Streptococcus gordonii, an oral commensal and opportunistic pathogen of animals and humans. CshA binds the high-molecular-weight glycoprotein fibronectin (Fn) via an N-terminal non-repetitive region, and this protein-protein interaction has been proposed to promote S. gordonii colonization at multiple sites within the host. This 259-kDa polypeptide is organized in the form of a leader peptide (residues 1-41), a non-repetitive region (residues 42-778), 17 repeat domains (R1-R17, each about 101-aa residues), and a C-terminal cell wall anchor. The non-repetitive Fn-binding region of CshA in turn is composed of three distinct domains, designated as non-repetitive domain 1 (NR1, CshA(42-222)), non-repetitive domain 2 (NR2, CshA(223-540)), and non-repetitive domain 3 (NR3, CshA(582-814)). The NR2 domain of CshA is shown to adopt a globular structure with a lectin-like fold and a ligand-binding site on its surface with structural homologues identified as those involved in binding carbohydrates or glycoproteins [1]. [1]. 27920201. The Streptococcus gordonii Adhesin CshA Protein Binds Host Fibronectin via a Catch-Clamp Mechanism. Back CR, Sztukowska MN, Till M, Lamont RJ, Jenkinson HF, Nobbs AH, Race PR;. J Biol Chem. 2017;292:1538-1549. (from Pfam)

Date:

2024-10-16

Lectins are structurally diverse proteins that bind to specific carbohydrates. This family includes the VIP36 Swiss:P49256 and ERGIC-53 Swiss:P49257 lectins. These two proteins were the first recognised members of a family of animal lectins similar (19-24%) to the leguminous plant lectins [1]. The alignment for this family aligns residues lying towards the N-terminus, where the similarity of VIP36 and ERGIC-53 is greatest. However, while Fiedler and Simons [1] identified these proteins as a new family of animal lectins, our alignment also includes yeast sequences. ERGIC-53 is a 53kD protein, localised to the intermediate region between the endoplasmic reticulum and the Golgi apparatus (ER-Golgi-Intermediate Compartment, ERGIC). It was identified as a calcium-dependent, mannose-specific lectin [2]. Its dysfunction has been associated with combined factors V and VIII deficiency OMIM:227300 OMIM:601567, suggesting an important and substrate-specific role for ERGIC-53 in the glycoprotein- secreting pathway [2,3]. [1]. 8205612. A putative novel class of animal lectins in the secretory pathway homologous to leguminous lectins. Fiedler K, Simons K;. Cell 1994;77:625-626. [2]. 8868475. ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins. Itin C, Roche AC, Monsigny M, Hauri HP;. Mol Biol Cell 1996;7:483-493. [3]. 10090935. ERGIC-53 gene structure and mutation analysis in 19 combined factors V and VIII deficiency families. Nichols WC, Terry VH, Wheatley MA, Yang A, Zivelin A, Ciavarella N, Stefanile C, Matsushita T, Saito H, de Bosch NB, Ruiz-Saez A, Torres A, Thompson AR, Feinstein. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16