1GSM
A reassessment of the MAdCAM-1 structure and its role in integrin recognition.
Summary for 1GSM
| Entry DOI | 10.2210/pdb1gsm/pdb |
| Related | 1BQS |
| Descriptor | MUCOSAL ADDRESSIN CELL ADHESION MOLECULE-1 (2 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) |
| Total number of polymer chains | 1 |
| Total formula weight | 22294.30 |
| Authors | Dando, J.,Wilkinson, K.W.,Ortlepp, S.,King, D.J.,Brady, R.L. (deposition date: 2002-01-08, release date: 2002-01-29, Last modification date: 2024-10-23) |
| Primary citation | Dando, J.,Wilkinson, K.W.,Ortlepp, S.,King, D.J.,Brady, R.L. A Reassessment of the Madcam-1 Structure and its Role in Integrin Recognition Acta Crystallogr.,Sect.D, 58:233-, 2002 Cited by PubMed Abstract: Mucosal addressin cell-adhesion molecule (MAdCAM-1) is a membrane-bound leukocyte receptor regulating both the passage and retention of leukocytes in mucosal tissues. A crystal structure for the two extracellular amino-terminal domains of human MAdCAM-1 has previously been reported, confirming their expected immunoglobulin superfamily topology. In this study, a second crystal structure of this fragment is described. Although the overall structure is similar to that previously reported, one edge strand in the amino-terminal domain is instead located on the opposite sheet. This alters the arrangement and conformation of amino acids in this region that have previously been shown to be crucial for ligand binding. MAdCAM-1 is also seen to form dimers within the crystal lattice, raising the possibility that oligomerization may influence the biological role of this adhesion molecule. PubMed: 11807247DOI: 10.1107/S0907444901020522 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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