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1jdp
From Proteopedia
| 1jdp, resolution 2.00Å () | |||||||||
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| Ligands: | , , | ||||||||
| Domains: | ANF_receptor, LivK | ||||||||
| Related: | 1jdn | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Crystal Structure of Hormone/Receptor Complex
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.
Allosteric activation of a spring-loaded natriuretic peptide receptor dimer by hormone., He Xl, Chow Dc, Martick MM, Garcia KC, Science. 2001 Aug 31;293(5535):1657-62. PMID:11533490
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1JDP is a 3 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- He Xl, Chow Dc, Martick MM, Garcia KC. Allosteric activation of a spring-loaded natriuretic peptide receptor dimer by hormone. Science. 2001 Aug 31;293(5535):1657-62. PMID:11533490 doi:10.1126/science.1062246
Page seeded by OCA on Wed Feb 18 00:37:55 2009
