1JDN
Crystal Structure of Hormone Receptor
Summary for 1JDN
Entry DOI | 10.2210/pdb1jdn/pdb |
Related | 1JDP |
Descriptor | ATRIAL NATRIURETIC PEPTIDE CLEARANCE RECEPTOR, beta-D-mannopyranose-(1-4)-alpha-D-mannopyranose-(1-4)-[beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
Functional Keywords | natriuretic peptide receptor, dimer, allosteric activation, signaling protein |
Biological source | Homo sapiens (human) |
Cellular location | Membrane; Single-pass type I membrane protein: P17342 |
Total number of polymer chains | 1 |
Total formula weight | 51580.50 |
Authors | He, X.-L.,Chow, D.-C.,Martick, M.M.,Garcia, K.C. (deposition date: 2001-06-14, release date: 2001-09-05, Last modification date: 2024-10-30) |
Primary citation | He, X.l.,Chow, D.c.,Martick, M.M.,Garcia, K.C. Allosteric activation of a spring-loaded natriuretic peptide receptor dimer by hormone. Science, 293:1657-1662, 2001 Cited by PubMed Abstract: Natriuretic peptides (NPs) are vasoactive cyclic-peptide hormones important in blood pressure regulation through interaction with natriuretic cell-surface receptors. We report the hormone-binding thermodynamics and crystal structures at 2.9 and 2.0 angstroms, respectively, of the extracellular domain of the unliganded human NP receptor (NPR-C) and its complex with CNP, a 22-amino acid NP. A single CNP molecule is bound in the interface of an NPR-C dimer, resulting in asymmetric interactions between the hormone and the symmetrically related receptors. Hormone binding induces a 20 angstrom closure between the membrane-proximal domains of the dimer. In each monomer, the opening of an interdomain cleft, which is tethered together by a linker peptide acting as a molecular spring, is likely a conserved allosteric trigger for intracellular signaling by the natriuretic receptor family. PubMed: 11533490DOI: 10.1126/science.1062246 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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