1i8y
From Proteopedia
(New page: 200px<br /><applet load="1i8y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i8y" /> '''SEMI-AUTOMATIC STRUCTURE DETERMINATION OF TH...) |
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'''SEMI-AUTOMATIC STRUCTURE DETERMINATION OF THE CG1 3-30 PEPTIDE BASED ON ARIA'''<br /> | '''SEMI-AUTOMATIC STRUCTURE DETERMINATION OF THE CG1 3-30 PEPTIDE BASED ON ARIA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Carp granulins are members of an emerging class of proteins with a | + | 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== | ==About this Structure== | ||
| - | 1I8Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1I8Y is a [http://en.wikipedia.org/wiki/Single_protein 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=1I8Y OCA]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11870861 11870861] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11870861 11870861] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bennett, H | + | [[Category: Bennett, H P.J.]] |
[[Category: James, S.]] | [[Category: James, S.]] | ||
[[Category: Ni, F.]] | [[Category: Ni, F.]] | ||
| - | [[Category: Vranken, W | + | [[Category: Vranken, W F.]] |
[[Category: beta-hairpin stack]] | [[Category: beta-hairpin stack]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:09:14 2008'' |
Revision as of 11:09, 21 February 2008
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SEMI-AUTOMATIC STRUCTURE DETERMINATION OF THE CG1 3-30 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
1I8Y is a Single protein structure of sequence from [1]. 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
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