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New page: left|200px<br /><applet load="1i8x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i8x" /> '''SEMI-AUTOMATIC STRUCTURE DETERMINATION OF TH...
 
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[[Image:1i8x.jpg|left|200px]]<br /><applet load="1i8x" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1i8x" />
'''SEMI-AUTOMATIC STRUCTURE DETERMINATION OF THE CG1 1-30 PEPTIDE BASED ON ARIA'''<br />


==Overview==
==SEMI-AUTOMATIC STRUCTURE DETERMINATION OF THE CG1 1-30 PEPTIDE BASED ON ARIA==
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.
<StructureSection load='1i8x' size='340' side='right'caption='[[1i8x]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1i8x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cyprinus_carpio Cyprinus carpio]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I8X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I8X FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1i8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i8x OCA], [https://pdbe.org/1i8x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i8x RCSB], [https://www.ebi.ac.uk/pdbsum/1i8x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i8x ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GRN1_CYPCA GRN1_CYPCA] Granulins have possible cytokine-like activity. They may play a role in inflammation, wound repair, and tissue remodeling.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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==
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<ref>PMID:11870861</ref>
1I8X 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I8X OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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]
</div>
[[Category: Single protein]]
<div class="pdbe-citations 1i8x" style="background-color:#fffaf0;"></div>
[[Category: Bennett, H.P.J.]]
== References ==
[[Category: James, S.]]
<references/>
[[Category: Ni, F.]]
__TOC__
[[Category: Vranken, W.F.]]
</StructureSection>
[[Category: two beta-hairpin stack]]
[[Category: Cyprinus carpio]]
 
[[Category: Large Structures]]
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:10:01 2007''
[[Category: Bennett HPJ]]
[[Category: James S]]
[[Category: Ni F]]
[[Category: Vranken WF]]
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