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1jdn
From Proteopedia
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|PDB= 1jdn |SIZE=350|CAPTION= <scene name='initialview01'>1jdn</scene>, resolution 2.9Å | |PDB= 1jdn |SIZE=350|CAPTION= <scene name='initialview01'>1jdn</scene>, resolution 2.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | + | |LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1jdp|1JDP]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jdn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jdn OCA], [http://www.ebi.ac.uk/pdbsum/1jdn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jdn RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=108962 108962]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: He, X L.]] | [[Category: He, X L.]] | ||
[[Category: Martick, M M.]] | [[Category: Martick, M M.]] | ||
| - | [[Category: CL]] | ||
[[Category: allosteric activation]] | [[Category: allosteric activation]] | ||
[[Category: crystal structure]] | [[Category: crystal structure]] | ||
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[[Category: natriuretic peptide receptor]] | [[Category: natriuretic peptide receptor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:32:07 2008'' |
Revision as of 18:32, 30 March 2008
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| , resolution 2.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , | ||||||
| Related: | 1JDP
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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.
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
Page seeded by OCA on Sun Mar 30 21:32:07 2008
