From Proteopedia
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| - | [[Image:1i8x.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1i8x| PDB=1i8x | SCENE= }} | | {{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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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11870861}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11870861 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11870861}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1I8X is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I8X OCA]. | + | 1I8X is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I8X OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Vranken, W F.]] | | [[Category: Vranken, W F.]] |
| | [[Category: Two beta-hairpin stack]] | | [[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 Tue Jul 1 10:35:52 2008'' |
Revision as of 07:35, 1 July 2008
Template:STRUCTURE 1i8x
SEMI-AUTOMATIC STRUCTURE DETERMINATION OF THE CG1 1-30 PEPTIDE BASED ON ARIA
Template:ABSTRACT PUBMED 11870861
About this Structure
1I8X is a Single protein structure. Full experimental 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 Tue Jul 1 10:35:52 2008
