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1yk1

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Revision as of 06:48, 25 April 2018

structure of natriuretic peptide receptor-C complexed with brain natriuretic peptide

Structural highlights

1yk1 is a 3 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1yk0
Gene:	NPR3, ANPRC (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ANPRC_HUMAN] Receptor for the natriuretic peptide hormones, binding with similar affinities atrial natriuretic peptide NPPA/ANP, brain natriuretic peptide NPPB/BNP, and C-type natriuretic peptide NPPC/CNP. May function as a clearance receptor for NPPA, NPPB and NPPC, regulating their local concentrations and effects. May regulate diuresis, blood pressure and skeletal development. Does not have guanylate cyclase activity. [ANFB_HUMAN] Cardiac hormone which may function as a paracrine antifibrotic factor in the heart. Also plays a key role in cardiovascular homeostasis through natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. Specifically binds and stimulates the cGMP production of the NPR1 receptor. Binds the clearance receptor NPR3.^[1]

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

Cardiovascular homeostasis and blood pressure regulation are reliant, in part, on interactions between natriuretic peptide (NP) hormones and natriuretic peptide receptors (NPR). The C-type NPR (NPR-C) is responsible for clearance of NP hormones from the circulation, and displays a cross-reactivity for all NP hormones (ANP, BNP, and CNP), in contrast to other NPRs, which are more restricted in their specificity. In order to elucidate the structural determinants for the binding specificity and cross-reactivity of NPR-C with NP hormones, we have determined the crystal structures of the complexes of NPR-C with atrial natriuretic peptide (ANP), and with brain natriuretic peptide (BNP). A structural comparison of these complexes, with the previous structure of the NPR-C/CNP complex, reveals that NPR-C uses a conformationally inflexible surface to bind three different, highly flexible, NP ligands. The complex structures support a mechanism of rigid promiscuity rather than conformational plasticity by the receptor. While ANP and BNP appear to adopt similar receptor-bound conformations, the CNP structure diverges, yet shares sets of common receptor contacts with the other ligands. The degenerate versus selective hormone recognition properties of different NPRs appears to derive largely from two cavities on the receptor surfaces, pocket I and pocket II, that serve as anchoring sites for hormone side-chains and modulate receptor selectivity.

Structural determinants of natriuretic peptide receptor specificity and degeneracy.,He XL, Dukkipati A, Garcia KC J Mol Biol. 2006 Aug 25;361(4):698-714. Epub 2006 Jul 10. PMID:16870210^[2]

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

References

↑ Koller KJ, Lowe DG, Bennett GL, Minamino N, Kangawa K, Matsuo H, Goeddel DV. Selective activation of the B natriuretic peptide receptor by C-type natriuretic peptide (CNP). Science. 1991 Apr 5;252(5002):120-3. PMID:1672777
↑ He XL, Dukkipati A, Garcia KC. Structural determinants of natriuretic peptide receptor specificity and degeneracy. J Mol Biol. 2006 Aug 25;361(4):698-714. Epub 2006 Jul 10. PMID:16870210 doi:10.1016/j.jmb.2006.06.060

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/1yk1"

@@ Line 1: / Line 1: @@
 ==structure of natriuretic peptide receptor-C complexed with brain natriuretic peptide==
 <StructureSection load='1yk1' size='340' side='right' caption='[[1yk1]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yk0|1yk0]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NPR3, ANPRC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1yk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yk1 OCA], [http://pdbe.org/1yk1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yk1 RCSB], [http://www.ebi.ac.uk/pdbsum/1yk1 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=1yk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yk1 OCA], [http://pdbe.org/1yk1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yk1 RCSB], [http://www.ebi.ac.uk/pdbsum/1yk1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1yk1 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yk/1yk1_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yk/1yk1_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1yk1

From Proteopedia

Revision as of 06:48, 25 April 2018

structure of natriuretic peptide receptor-C complexed with brain natriuretic peptide

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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