Structural analysis of a non-redundant data set of 47 immunoglobulin (Ig) proteins was carried out using a combination of criteria: atom--atom contact compatibility, position occupancy rate, conservation of residue type and positional conservation in 3D space. Our analysis shows that roughly half of the interface positions between the light and heavy chains are specific to individual structures while the other half are conserved across the database. The tendency for conservation of a primary subset of positions holds true for the intra-domain faces as well. These subsets, with an average of 12 conserved positions and a contact surface of 630 A(2), delineate the inter- and intra-domain core, a refined instrument with a reduced target for analysis of sheet--sheet interactions in sandwich-like proteins. Employing this instrument, we find that a majority of Ig interface core positions are adjoined in sequence to domain core positions. This was derived independent of geometric considerations, however beta-sheet side-chain geometry clearly dictates it. The geometric wedding of the domain and interface cores supports the concept of a rigid-like substructure on the protein surface involved in complex formation and indicates a close relationship between surface determinants and those involved in protein folding of Ig domains. The definitions developed for the Ig interface and domain cores proved satisfactory to extract first-approximation cores for a group of 24 non-Ig sandwich-like proteins, treated as individual structures due to their diverse strand topologies. We show that the same rule of positional connectivity between the rigid domain core and interface core extends generally to sandwich-like proteins interacting in a sheet--sheet fashion. The non-Ig structures were used as templates to analyze sandwich-like interfaces of unresolved homologous proteins using a database merging structure and sequence conservation.