1ANP: SOLUTION CONFORMATION OF AN ATRIAL NATRIURETIC PEPTIDE VARIANT SELECTIVE FOR THE TYPE-A RECEPTOR

Citation:
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.
PDB ID: 1ANPDownload
MMDB ID: 55289
PDB Deposition Date: 1994/4/6
Updated in MMDB: 2007/10
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 1ANP: monomeric; determined by author
Molecular Components in 1ANP
Label Count Molecule
Protein (1 molecule)
1
Atrial Natriuretic Peptide(Gene symbol: NPPA)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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