1BY2
STRUCTURE OF M2BP SCAVENGER RECEPTOR CYSTEINE-RICH DOMAIN
Summary for 1BY2
| Entry DOI | 10.2210/pdb1by2/pdb |
| Descriptor | MAC-2 BINDING PROTEIN, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
| Functional Keywords | extracellular module, scavenger receptor, tumour-associated antigen, extracellular matrix, glycosylated protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 12926.30 |
| Authors | Hohenester, E.,Sasaki, T.,Timpl, R. (deposition date: 1998-10-23, release date: 1999-05-18, Last modification date: 2024-11-20) |
| Primary citation | Hohenester, E.,Sasaki, T.,Timpl, R. Crystal structure of a scavenger receptor cysteine-rich domain sheds light on an ancient superfamily. Nat.Struct.Biol., 6:228-232, 1999 Cited by PubMed Abstract: Scavenger receptor cysteine-rich (SRCR) domains are found widely in cell surface molecules and in some secreted proteins, where they are thought to mediate ligand binding. We have determined the crystal structure at 2.0 A resolution of the SRCR domain of Mac-2 binding protein (M2BP), a tumor-associated antigen and matrix protein. The structure reveals a curved six-stranded beta-sheet cradling an alpha-helix. Structure-based sequence alignment demonstrates that the M2BP SRCR domain is a valid template for the entire SRCR protein superfamily. This allows an interpretation of previous mutagenesis data on ligand binding to the lymphocyte receptor CD6. PubMed: 10074941DOI: 10.1038/6669 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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