1anp

SOLUTION CONFORMATION OF AN ATRIAL NATRIURETIC PEPTIDE VARIANT SELECTIVE FOR THE TYPE-A RECEPTORSOLUTION CONFORMATION OF AN ATRIAL NATRIURETIC PEPTIDE VARIANT SELECTIVE FOR THE TYPE-A RECEPTOR

Structural highlights

1anp is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

ANF_HUMAN Defects in NPPA are the cause of familial atrial fibrillation type 6 (ATFB6) [MIM:612201. Atrial fibrillation is a common disorder of cardiac rhythm that is hereditary in a small subgroup of patients. It is characterized by disorganized atrial electrical activity, progressive deterioration of atrial electromechanical function and ineffective pumping of blood into the ventricles. It can be associated with palpitations, syncope, thromboembolic stroke, and congestive heart failure.^[1]

Function

ANF_HUMAN Hormone playing a key role in cardiovascular homeostasis through regulation of natriuresis, diuresis, and vasodilation. Also plays a role in female pregnancy by promoting trophoblast invasion and spiral artery remodeling in uterus. Specifically binds and stimulates the cGMP production of the NPR1 receptor. Binds the clearance receptor NPR3.^[2]

Publication Abstract from PubMed

Two-dimensional NMR spectroscopy has been used to characterize the solution conformation of an atrial natriuretic peptide (ANP) variant which is selective for the human natriuretic peptide receptor A (NPR-A) relative to receptor C (NPR-C). The ANP mutant, containing six substitutions, has reduced flexibility in aqueous solution relative to wild-type ANP and allows the observation of sufficient NOE connectivities for structure determination by distance geometry and restrained molecular dynamics calculations. The solution conformation is reasonably well defined, having an average backbone atom rms deviation from the average coordinates of approximately 1.1 A for residues 7-27. The structure is consistent with available functional data and shows a spatial separation between known receptor binding determinants and residues found to be outside the hormone-receptor interface.

Solution conformation of an atrial natriuretic peptide variant selective for the type A receptor.,Fairbrother WJ, McDowell RS, Cunningham BC Biochemistry. 1994 Aug 2;33(30):8897-904. PMID:8043577^[3]

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

References

↑ Hodgson-Zingman DM, Karst ML, Zingman LV, Heublein DM, Darbar D, Herron KJ, Ballew JD, de Andrade M, Burnett JC Jr, Olson TM. Atrial natriuretic peptide frameshift mutation in familial atrial fibrillation. N Engl J Med. 2008 Jul 10;359(2):158-65. PMID:18614783 doi:359/2/158
↑ 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
↑ Fairbrother WJ, McDowell RS, Cunningham BC. Solution conformation of an atrial natriuretic peptide variant selective for the type A receptor. Biochemistry. 1994 Aug 2;33(30):8897-904. PMID:8043577

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OCA

[1] Hodgson-Zingman DM, Karst ML, Zingman LV, Heublein DM, Darbar D, Herron KJ, Ballew JD, de Andrade M, Burnett JC Jr, Olson TM. Atrial natriuretic peptide frameshift mutation in familial atrial fibrillation. N Engl J Med. 2008 Jul 10;359(2):158-65. PMID:18614783 doi:359/2/158

[2] 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

[3] Fairbrother WJ, McDowell RS, Cunningham BC. Solution conformation of an atrial natriuretic peptide variant selective for the type A receptor. Biochemistry. 1994 Aug 2;33(30):8897-904. PMID:8043577

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