1BQS
THE CRYSTAL STRUCTURE OF MUCOSAL ADDRESSIN CELL ADHESION MOLECULE-1 (MADCAM-1)
Summary for 1BQS
Entry DOI | 10.2210/pdb1bqs/pdb |
Descriptor | PROTEIN (MUCOSAL ADDRESSIN CELL ADHESION MOLECULE-1), 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
Functional Keywords | cell adhesion protein, madcam-1, immunoglobulin fold, i-set fold, cell adhesion glycoprotein, integrin recoginition, membrane protein |
Biological source | Homo sapiens (human) |
Cellular location | Membrane; Single-pass type I membrane protein: Q13477 |
Total number of polymer chains | 1 |
Total formula weight | 22339.25 |
Authors | Tan, K.,Casasnovas, J.M.,Liu, J.H.,Briskin, M.J.,Springer, T.A.,Wang, J.-H. (deposition date: 1998-08-18, release date: 1999-08-13, Last modification date: 2024-11-13) |
Primary citation | Tan, K.,Casasnovas, J.M.,Liu, J.H.,Briskin, M.J.,Springer, T.A.,Wang, J.H. The structure of immunoglobulin superfamily domains 1 and 2 of MAdCAM-1 reveals novel features important for integrin recognition. Structure, 6:793-801, 1998 Cited by PubMed Abstract: Mucosal addressin cell adhesion molecule 1 (MAdCAM-1) is a cell adhesion molecule that is expressed on the endothelium in mucosa, and guides the specific homing of lymphocytes into mucosal tissues. MAdCAM-1 belongs to a subclass of the immunoglobulin superfamily (IgSF), the members of which are ligands for integrins. Human MAdCAM-1 has a unique dual function compared to other members in the same subclass in that it binds both the integrin alpha4beta7, through its two IgSF domains, and a selectin expressed on leukocytes, via carbohydrate sidechains. The structure determination of the two IgSF domains and comparison to the N-terminal two-domain structures of vascular cell adhesion molecule 1 (VCAM-1) and intercellular adhesion molecules (ICAM-1 and ICAM-2) allow us to assess the molecular basis of the interactions between integrins and their preferred ligands. PubMed: 9655832DOI: 10.1016/S0969-2126(98)00080-X PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
Download full validation report
