1qgm: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1qgm.jpg|left|200px]] | [[Image:1qgm.jpg|left|200px]] | ||
'''THE SOLUTION STRUCTURE OF A 30 RESIDUE AMINO-TERMINAL DOMAIN OF THE CARP GRANULIN-1 PROTEIN.''' | {{Structure | ||
|PDB= 1qgm |SIZE=350|CAPTION= <scene name='initialview01'>1qgm</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''THE SOLUTION STRUCTURE OF A 30 RESIDUE AMINO-TERMINAL DOMAIN OF THE CARP GRANULIN-1 PROTEIN.''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1QGM is a [ | 1QGM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QGM OCA]. | ||
==Reference== | ==Reference== | ||
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., Vranken WF, Chen ZG, Xu P, James S, Bennett HP, Ni F, J Pept Res. 1999 May;53(5):590-7. PMID:[http:// | 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., Vranken WF, Chen ZG, Xu P, James S, Bennett HP, Ni F, J Pept Res. 1999 May;53(5):590-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10424355 10424355] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ni, F.]] | [[Category: Ni, F.]] | ||
| Line 18: | Line 27: | ||
[[Category: conformational stability]] | [[Category: conformational stability]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:37:10 2008'' | ||
Revision as of 14:37, 20 March 2008
| |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE SOLUTION STRUCTURE OF A 30 RESIDUE AMINO-TERMINAL DOMAIN OF THE CARP GRANULIN-1 PROTEIN.
OverviewOverview
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.
About this StructureAbout this Structure
1QGM is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
ReferenceReference
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., Vranken WF, Chen ZG, Xu P, James S, Bennett HP, Ni F, J Pept Res. 1999 May;53(5):590-7. PMID:10424355
Page seeded by OCA on Thu Mar 20 13:37:10 2008