1ANP

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

Summary for 1ANP

• Entry DOI: 10.2210/pdb1anp/pdb
• Descriptor: ATRIAL NATRIURETIC PEPTIDE (1 entity in total)
• Functional Keywords: hypotensive hormone
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P01160
• Total number of polymer chains: 1
• Total formula weight: 3031.32

Authors

Fairbrother, W.J.,Mcdowell, R.S.,Cunningham, B.C. (deposition date: 1994-04-06, release date: 1995-04-07, Last modification date: 2024-04-10)

Primary citation

Fairbrother, W.J.,McDowell, R.S.,Cunningham, B.C.
Solution conformation of an atrial natriuretic peptide variant selective for the type A receptor.
Biochemistry, 33:8897-8904, 1994

PubMed Abstract: 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.

PubMed: 8043577
DOI: 10.1021/bi00196a006

Experimental method

SOLUTION NMR