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1dp4

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Revision as of 07:23, 25 October 2017

DIMERIZED HORMONE BINDING DOMAIN OF THE ATRIAL NATRIURETIC PEPTIDE RECEPTOR

Structural highlights

1dp4 is a 2 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Activity:	Guanylate cyclase, with EC number 4.6.1.2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ANPRA_RAT] Receptor for the atrial natriuretic peptide NPPA/ANP and the brain natriuretic peptide NPPB/BNP which are potent vasoactive hormones playing a key role in cardiovascular homeostasis. Has guanylate cyclase activity upon binding of the ligand (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The atrial natriuretic peptide (ANP) hormone is secreted by the heart in response to an increase in blood pressure. ANP exhibits several potent anti-hypertensive actions in the kidney, adrenal gland and vascular system. These actions are induced by hormone binding extracellularly to the ANP receptor, thereby activating its intracellular guanylyl cyclase domain for the production of cyclic GMP. Here we present the crystal structure of the glycosylated dimerized hormone-binding domain of the ANP receptor at 2.0-A resolution. The monomer comprises two interconnected subdomains, each encompassing a central beta-sheet flanked by alpha-helices, and exhibits the type I periplasmic binding protein fold. Dimerization is mediated by the juxtaposition of four parallel helices, arranged two by two, which brings the two protruding carboxy termini into close relative proximity. From affinity labelling and mutagenesis studies, the ANP-binding site maps to the side of the dimer crevice and extends to near the dimer interface. A conserved chloride-binding site is located in the membrane distal domain, and we found that hormone binding is chloride dependent. These studies suggest mechanisms for hormone activation and the allostery of the ANP receptor.

Structure of the dimerized hormone-binding domain of a guanylyl-cyclase-coupled receptor.,van den Akker F, Zhang X, Miyagi M, Huo X, Misono KS, Yee VC Nature. 2000 Jul 6;406(6791):101-4. PMID:10894551^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ van den Akker F, Zhang X, Miyagi M, Huo X, Misono KS, Yee VC. Structure of the dimerized hormone-binding domain of a guanylyl-cyclase-coupled receptor. Nature. 2000 Jul 6;406(6791):101-4. PMID:10894551 doi:10.1038/35017602

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dp4"

@@ Line 1: / Line 1: @@
 ==DIMERIZED HORMONE BINDING DOMAIN OF THE ATRIAL NATRIURETIC PEPTIDE RECEPTOR==
 <StructureSection load='1dp4' size='340' side='right' caption='[[1dp4]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Guanylate_cyclase Guanylate cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.2 4.6.1.2] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dp4 OCA], [http://pdbe.org/1dp4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dp4 RCSB], [http://www.ebi.ac.uk/pdbsum/1dp4 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dp4 OCA], [http://pdbe.org/1dp4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dp4 RCSB], [http://www.ebi.ac.uk/pdbsum/1dp4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dp4 ProSAT]</span></td></tr>
 </table>
 == Function ==

1dp4

From Proteopedia

Revision as of 07:23, 25 October 2017

DIMERIZED HORMONE BINDING DOMAIN OF THE ATRIAL NATRIURETIC PEPTIDE RECEPTOR

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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