1i8x: Difference between revisions

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[[Image:1i8x.jpg|left|200px]]
{{Seed}}
[[Image:1i8x.png|left|200px]]


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{{STRUCTURE_1i8x|  PDB=1i8x  |  SCENE=  }}  
{{STRUCTURE_1i8x|  PDB=1i8x  |  SCENE=  }}  


'''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===




==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}}


==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].  


==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

File:1i8x.png

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

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