1QGM
THE SOLUTION STRUCTURE OF A 30 RESIDUE AMINO-TERMINAL DOMAIN OF THE CARP GRANULIN-1 PROTEIN.
Summary for 1QGM
| Entry DOI | 10.2210/pdb1qgm/pdb |
| NMR Information | BMRB: 4351 |
| Descriptor | PROTEIN (AMINO-TERMINAL CARP GRANULIN-1) (1 entity in total) |
| Functional Keywords | beta-hairpin stack, conformational stability, cytokine |
| Cellular location | Secreted: P81013 |
| Total number of polymer chains | 1 |
| Total formula weight | 3195.60 |
| Authors | Vranken, W.F.,Xu, P.,Ni, F. (deposition date: 1999-05-01, release date: 1999-12-22, Last modification date: 2024-11-20) |
| Primary citation | Vranken, W.F.,Chen, Z.G.,Xu, P.,James, S.,Bennett, H.P.,Ni, F. A 30-residue fragment of the carp granulin-1 protein folds into a stack of two beta-hairpins similar to that found in the native protein. J.Pept.Res., 53:590-597, 1999 Cited by PubMed Abstract: Upon air oxidation, a peptide corresponding to the 30-residue N-terminal subdomain of carp granulin-1 spontaneously formed the disulfide pairing observed in the native protein. Structural characterization using NMR showed the presence of a defined secondary structure within this peptide. The chemical shifts for most of the alphaCH protons of the peptide and the protein are very similar, and the observed NOE contacts of the peptide strongly resemble those in the protein. A structure calculation of the peptide using NOE distance constraints indicates that the peptide fragment adopts the same conformation as formed within the native protein. The 30-residue N-terminal peptide of carp granulin-1 is the first example of an independently folded stack of two beta-hairpins reinforced by two interhairpin disulfide bonds. Two key areas of the structure show a clustering of hydrophobic residues that may account for its exceptional conformational stability. PubMed: 10424355DOI: 10.1034/j.1399-3011.1999.00048.x PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
