1jdp
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1jdp.gif|left|200px]] | [[Image:1jdp.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1jdp", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_1jdp| PDB=1jdp | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Crystal Structure of Hormone/Receptor Complex''' | '''Crystal Structure of Hormone/Receptor Complex''' | ||
| Line 29: | Line 26: | ||
[[Category: He, X L.]] | [[Category: He, X L.]] | ||
[[Category: Martick, M M.]] | [[Category: Martick, M M.]] | ||
| - | [[Category: | + | [[Category: Allosteric activation]] |
| - | [[Category: | + | [[Category: Crystal structure]] |
| - | [[Category: | + | [[Category: Hormone/receptor complex]] |
| - | [[Category: | + | [[Category: Natriuretic peptide receptor]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:05:57 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 18:05, 2 May 2008
Crystal Structure of Hormone/Receptor Complex
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.
About this Structure
1JDP is a Protein complex structure of sequences from Homo sapiens. 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 Page seeded by OCA on Fri May 2 21:05:57 2008
