2NPL
NMR Structure of CARD d2 Domain
Summary for 2NPL
| Entry DOI | 10.2210/pdb2npl/pdb |
| Related | 1RSF |
| NMR Information | BMRB: 7291 |
| Descriptor | Coxsackievirus and Adenovirus Receptor (1 entity in total) |
| Functional Keywords | coxsakievirus and adenovirus receptor, cell adhesion |
| Biological source | Homo sapiens (human) |
| Cellular location | Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Cell membrane; Single-pass type I membrane protein. Isoform 3: Secreted. Isoform 4: Secreted. Isoform 5: Secreted: P78310 |
| Total number of polymer chains | 1 |
| Total formula weight | 10539.77 |
| Authors | Jiang, S.,Caffrey, M. (deposition date: 2006-10-27, release date: 2007-03-13, Last modification date: 2024-10-30) |
| Primary citation | Jiang, S.,Caffrey, M. Solution structure of the coxsackievirus and adenovirus receptor domain 2 Protein Sci., 16:539-542, 2007 Cited by PubMed Abstract: The coxsackievirus and adenovirus receptor (CAR) mediates entry of coxsackievirus and adenovirus. CAR possesses an extracellular region that is comprised of 2 immunoglobulin domains termed CAR-D1 and CAR-D2. In the present work, the solution structure of CAR-D2, consisting of residues 142-235 of human CAR, has been determined by NMR spectroscopy. CAR-D2 is shown to be a beta-sandwich motif comprised of two beta-sheets, which are stabilized by two disulfide bonds. The first beta-sheet is comprised of beta-strands A, B, and E, and the second beta-sheet is comprised of beta-strands C, F, and G. A relatively hydrophobic helix is found between beta-strands C and E, which replaces beta-strand D of the classical c-type immunoglobulin fold. PubMed: 17322536DOI: 10.1110/ps.062643507 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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