1jdn: Difference between revisions
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[[Image:1jdn.gif|left|200px]] | [[Image:1jdn.gif|left|200px]] | ||
'''Crystal Structure of Hormone Receptor''' | {{Structure | ||
|PDB= 1jdn |SIZE=350|CAPTION= <scene name='initialview01'>1jdn</scene>, resolution 2.9Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal Structure of Hormone Receptor''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1JDN is a [ | 1JDN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDN OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11533490 11533490] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: natriuretic peptide receptor]] | [[Category: natriuretic peptide receptor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:01:59 2008'' | ||
Revision as of 10:02, 20 March 2008
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| 1jdn, resolution 2.9Å | |||||||||||||
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| Ligands: | CL | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Crystal Structure of Hormone Receptor
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
1JDN is a Single protein structure of sequence 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
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