1JDP

Crystal Structure of Hormone/Receptor Complex

Summary for 1JDP

• Entry DOI: 10.2210/pdb1jdp/pdb
• Related: 1JDN
• Descriptor: ATRIAL NATRIURETIC PEPTIDE CLEARANCE RECEPTOR, C-TYPE NATRIURETIC PEPTIDE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: hormone-receptor complex, natriuretic peptide receptor, allosteric activation, signaling protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 3
• Total formula weight: 102445.19

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: 2024-11-13)

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

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: 11533490
DOI: 10.1126/science.1062246

Experimental method

X-RAY DIFFRACTION (2 Å)