1jdp
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(New page: 200px<br /> <applet load="1jdp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jdp, resolution 2.0Å" /> '''Crystal Structure of...)
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Revision as of 15:33, 12 November 2007
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Crystal Structure of Hormone/Receptor Complex
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Hypertension, salt-resistant (1) OMIM:[108962]
About this Structure
1JDP is a Protein complex structure of sequences from Homo sapiens with NDG, NAG and CL as ligands. Full crystallographic information is available from OCA.
Reference
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
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