Protein Family Models

Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains. Review of LRR proteins. [1]. 7817399. The leucine-rich repeat: a versatile binding motif.. Kobe B, Deisenhofer J;. Trends Biochem Sci 1994;19:415-421. (from Pfam)

Date:

2024-04-03

This domain family is found in bacteria, and is approximately 60 amino acids in length. The family is found in association with Pfam:PF00560, Pfam:PF08191, Pfam:PF09479. There are two completely conserved residues (I and F) that may be functionally important. Internalin mediates bacterial adhesion and invasion of epithelial cells in the human intestine through specific interaction with its host cell receptor E-cadherin. This family is the N terminal of internalin, the cap domain of the protein. The cap domain is conserved between different internalin types. The cap domain does not interact with E cadherin, therefore its function is presumably structural: capping the hydrophobic core. [1]. 12526809. Structure of internalin, a major invasion protein of Listeria. monocytogenes, in complex with its human receptor E-cadherin.. Schubert WD, Urbanke C, Ziehm T, Beier V, Machner MP, Domann E,. Wehland J, Chakraborty T, Heinz DW;. Cell 2002;111:825-836. (from Pfam)

Date:

2024-04-03

These are small, all beta strand domains, structurally described for the protein Internalin (InlA) and related proteins InlB, InlE, InlH from the pathogenic bacterium Listeria monocytogenes. Their function appears to be mainly structural: They are fused to the C-terminal end of leucine-rich repeats (LRR), significantly stabilising the LRR, and forming a common rigid entity with the LRR. They are themselves not involved in protein-protein-interactions but help to present the adjacent LRR-domain for this purpose. These domains belong to the family of Ig-like domains in that they consist of two sandwiched beta sheets that follow the classical connectivity of Ig-domains. The beta strands in one of the sheets is, however, much smaller than in most standard Ig-like domains, making it somewhat of an outlier [1],[2] [3]. [1]. 11575932. Internalins from the human pathogen Listeria monocytogenes. combine three distinct folds into a contiguous internalin. domain.. Schubert WD, Gobel G, Diepholz M, Darji A, Kloer D, Hain T,. Chakraborty T, Wehland J, Domann E, Heinz DW;. J Mol Biol 2001;312:783-794.. [2]. 12526809. Structure of internalin, a major invasion protein of Listeria. monocytogenes, in complex with its human receptor E-cadherin.. Schubert WD, Urbanke C, Ziehm T, Beier V, Machner MP, Domann E,. Wehland J, Chakraborty T, Heinz DW;. Cell 2002;111:825-836.. [3]. 15003459. Folding and stability of the leucine-rich repeat domain of. internalin B from Listeri monocytogenes.. Freiberg A, Machner MP, Pfeil W, Schubert WD, Heinz DW, Seckler. R;. J Mol Biol 2004;337:453-461. (from Pfam)

Date:

2024-04-03