1i8x
From Proteopedia
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| - | + | {{STRUCTURE_1i8x| PDB=1i8x | SCENE= }} | |
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'''SEMI-AUTOMATIC STRUCTURE DETERMINATION OF THE CG1 1-30 PEPTIDE BASED ON ARIA''' | '''SEMI-AUTOMATIC STRUCTURE DETERMINATION OF THE CG1 1-30 PEPTIDE BASED ON ARIA''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1I8X is a [[Single protein]] structure | + | 1I8X is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I8X OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ni, F.]] | [[Category: Ni, F.]] | ||
[[Category: Vranken, W F.]] | [[Category: Vranken, W F.]] | ||
| - | [[Category: | + | [[Category: Two beta-hairpin stack]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:43:06 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 16:43, 2 May 2008
SEMI-AUTOMATIC STRUCTURE DETERMINATION OF THE CG1 1-30 PEPTIDE BASED ON ARIA
Overview
Carp granulins are members of an emerging class of proteins with a sequence motif encoding a parallel stack of two to four beta-hairpins. The carp granulin-1 protein forms a stack of four beta-hairpins, whereas its amino-terminal fragment appears to adopt a very stable stack of two beta-hairpins in solution. Here we determined a refined three-dimensional structure of this peptide fragment to examine potential conformational changes compared with the full-length protein. The structures were calculated with both a traditional method and a fast semiautomated method using ambiguous NMR distance restraints. The resulting sets of structures are very similar and show that a well-defined stack of two beta-hairpins is retained in the peptide. Conformational rearrangements compensating the loss of the carboxy-terminal subdomain of the native protein are restricted to the carboxy-terminal end of the peptide, the turn connecting the two beta-hairpins, and the Tyr(21) and Tyr(25) aromatic side chains. Further removal of the Val(1) and Ile(2) residues, which are part of the first beta-hairpin and components of two major hydrophobic clusters in the two beta-hairpin structure, results in the loss of the first beta-hairpin. The second beta-hairpin, which is closely associated with the first, retains a similar but somewhat less stable conformation. The invariable presence of the second beta-hairpin and the dependence of its stability on the first beta-hairpin suggest that the stack of two beta-hairpins may be an evolutionary conserved and autonomous folding unit. In addition, the high conformational stability makes the stack of two beta-hairpins an attractive scaffold for the development of peptide-based drug candidates.
About this Structure
1I8X is a Single protein structure. Full crystallographic information is available from OCA.
Reference
Solution structures of a 30-residue amino-terminal domain of the carp granulin-1 protein and its amino-terminally truncated 3-30 subfragment: implications for the conformational stability of the stack of two beta-hairpins., Vranken WF, James S, Bennett HP, Ni F, Proteins. 2002 Apr 1;47(1):14-24. PMID:11870861 Page seeded by OCA on Fri May 2 19:43:06 2008
