Lysosome-associated membrane glycoprotein

Lysosome-associated membrane glycoproteins (LAMPs)   are integral membrane proteins, specific to lysosomes, and whose exact biological function is not yet clear. Structurally, the lamp proteins consist of two internally homologous lysosome-luminal domains separated by a proline-rich hinge region; at the C-terminal extremity there is a transmembrane region (TM) followed by a very short cytoplasmic tail (C). In each of the duplicated domains, there are two conserved disulfide bonds. This structure is schematically represented in the figure below.

+-+           +-+         +-+            +-+   |     |            |     |         |     |            |     |  xCxxxxxCxxxxxxxxxxxxCxxxxxCxxxxxxxxxCxxxxxCxxxxxxxxxxxxCxxxxxCxxxxxxxx +--++Hinge++--++TM++C+

In mammals, there are two closely related types of LAMP: LAMP1 and LAMP2.

CD68 (also called gp110 or macrosialin) is a heavily glycosylated integral membrane protein whose structure consists of a mucin-like domain followed by a proline-rich hinge; a single LAMP-like domain; a transmembrane region and a short cytoplasmic tail.

CD molecules are leucocyte antigens on cell surfaces. CD antigen nomenclature is updated at Protein Reviews On The Web (https://web.archive.org/web/20080920090434/http://mpr.nci.nih.gov/prow/).

Human proteins containing this domain

 * CD68
 * LAMP1
 * LAMP2
 * LAMP3