The amino-terminal immunoglobulin-like domain of activated leukocyte cell adhesion molecule binds specifically to the membrane-proximal scavenger receptor cysteine-rich domain of CD6 with a 1:1 stoichiometry. Export

@article{citeulike:562077, abstract = {Activated leukocyte cell adhesion molecule (ALCAM) was recently identified as a ligand for CD6, a signaling receptor expressed on T cells, a subset of B cells, and some cells in the brain. Receptor-ligand binding assays, antibody blocking experiments, and examination of the tissue distribution of these two cell surface proteins suggest that CD6-ALCAM interactions play an important role in mediating the binding of thymocytes to thymic epithelial cells and of T cells to activated leukocytes. Presently, the details of CD6-ALCAM interactions and of signaling through CD6 are unknown. A series of truncated human ALCAM and CD6 immunoglobulin fusion proteins were produced and tested in different binding assays to analyze ALCAM-CD6 interactions in more detail. In this study, we report that the amino-terminal Ig-like domain of human ALCAM specifically binds to the third membrane-proximal scavenger receptor cysteine-rich (SRCR) domain of human CD6. Using thrombin-cleaved Ig fusion proteins containing single or multiple ALCAM or CD6 domains, we were able to determine that the stoichiometry of the interaction between the amino-terminal ALCAM domains and the membrane-proximal CD6 SRCR domain is 1:1. These results provide the first example of an Ig-like domain mediating an interaction with an SRCR domain.}, address = {Bristol-Myers Squibb Pharmaceutical Research Institute, Seattle, Washington 98121, USA.}, author = {Bowen, M. A. and Bajorath, J. and Siadak, A. W. and Modrell, B. and Malacko, A. R. and Marquardt, H. and Nadler, S. G. and Aruffo, A.}, citeulike-article-id = {562077}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/8663238}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=8663238}, day = {19}, issn = {0021-9258}, journal = {J Biol Chem}, keywords = {alcam, cd6, leucocyte, receptor}, month = {July}, number = {29}, pages = {17390--17396}, posted-at = {2006-03-24 08:50:19}, priority = {0}, title = {The amino-terminal immunoglobulin-like domain of activated leukocyte cell adhesion molecule binds specifically to the membrane-proximal scavenger receptor cysteine-rich domain of CD6 with a 1:1 stoichiometry.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/8663238}, volume = {271}, year = {1996} }

TY - JOUR ID - citeulike:562077 L3 - citeulike-article-id:562077 N2 - Activated leukocyte cell adhesion molecule (ALCAM) was recently identified as a ligand for CD6, a signaling receptor expressed on T cells, a subset of B cells, and some cells in the brain. Receptor-ligand binding assays, antibody blocking experiments, and examination of the tissue distribution of these two cell surface proteins suggest that CD6-ALCAM interactions play an important role in mediating the binding of thymocytes to thymic epithelial cells and of T cells to activated leukocytes. Presently, the details of CD6-ALCAM interactions and of signaling through CD6 are unknown. A series of truncated human ALCAM and CD6 immunoglobulin fusion proteins were produced and tested in different binding assays to analyze ALCAM-CD6 interactions in more detail. In this study, we report that the amino-terminal Ig-like domain of human ALCAM specifically binds to the third membrane-proximal scavenger receptor cysteine-rich (SRCR) domain of human CD6. Using thrombin-cleaved Ig fusion proteins containing single or multiple ALCAM or CD6 domains, we were able to determine that the stoichiometry of the interaction between the amino-terminal ALCAM domains and the membrane-proximal CD6 SRCR domain is 1:1. These results provide the first example of an Ig-like domain mediating an interaction with an SRCR domain. IS - 29 JF - J Biol Chem SN - 0021-9258 AD - Bristol-Myers Squibb Pharmaceutical Research Institute, Seattle, Washington 98121, USA. EP - 17396 TI - The amino-terminal immunoglobulin-like domain of activated leukocyte cell adhesion molecule binds specifically to the membrane-proximal scavenger receptor cysteine-rich domain of CD6 with a 1:1 stoichiometry. VL - 271 SP - 17390 KW - alcam KW - cd6 KW - leucocyte KW - receptor AU - Bowen, MA AU - Bajorath, J AU - Siadak, AW AU - Modrell, B AU - Malacko, AR AU - Marquardt, H AU - Nadler, SG AU - Aruffo, A PY - 1996/07/19/ UR - http://view.ncbi.nlm.nih.gov/pubmed/8663238 ER -