The Ig-like fold is part of proteins with important roles in different physiological processes [ PUBMED:16631788 ]. This entry represents the bacterial Ig-like domain (Big2). This domain is mainly found in a variety of bacterial and phage surface proteins such as intimins, but has also been found in several eukaryote … expand

The Ig-like fold is part of proteins with important roles in different physiological processes [ PUBMED:16631788 ]. This entry represents the bacterial Ig-like domain (Big2). This domain is mainly found in a variety of bacterial and phage surface proteins such as intimins, but has also been found in several eukaryote proteins [ PUBMED:14517331 ].

Intimin (Eae protein) is a bacterial cell-adhesion molecule that mediates the intimate bacterial host-cell interaction. It contains three domains; two immunoglobulin-like domains and a C-type lectin-like module implying that carbohydrate recognition may be important in intimin-mediated cell adhesion [ PUBMED:10201396 PUBMED:10890451 ].

The structure of this domain was also described in the Tail tube protein of phage lambda (TTP). This protein assembles in hexameric rings that stack on top of each others [ PUBMED:23911548 PUBMED:20826161 ].

Nuclear pore membrane glycoprotein 210 from humans (POM210) also belongs to this group of proteins. This nucleoporin is essential for nuclear pore assembly and fusion, nuclear pore spacing, as well as structural integrity [ PUBMED:14517331 ].