1gjz
From Proteopedia
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| - | [[Image:1gjz.jpg|left|200px]] | + | [[Image:1gjz.jpg|left|200px]] |
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| - | '''SOLUTION STRUCTURE OF A DIMERIC N-TERMINAL FRAGMENT OF HUMAN UBIQUITIN''' | + | {{Structure |
| + | |PDB= 1gjz |SIZE=350|CAPTION= <scene name='initialview01'>1gjz</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''SOLUTION STRUCTURE OF A DIMERIC N-TERMINAL FRAGMENT OF HUMAN UBIQUITIN''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GJZ is a [ | + | 1GJZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJZ OCA]. |
==Reference== | ==Reference== | ||
| - | Structure and properties of a dimeric N-terminal fragment of human ubiquitin., Bolton D, Evans PA, Stott K, Broadhurst RW, J Mol Biol. 2001 Dec 7;314(4):773-87. PMID:[http:// | + | Structure and properties of a dimeric N-terminal fragment of human ubiquitin., Bolton D, Evans PA, Stott K, Broadhurst RW, J Mol Biol. 2001 Dec 7;314(4):773-87. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11733996 11733996] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ubiquitin]] | [[Category: ubiquitin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:24:08 2008'' |
Revision as of 09:24, 20 March 2008
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SOLUTION STRUCTURE OF A DIMERIC N-TERMINAL FRAGMENT OF HUMAN UBIQUITIN
Contents |
Overview
Previous peptide dissection and kinetic experiments have indicated that in vitro folding of ubiquitin may proceed via transient species in which native-like structure has been acquired in the first 45 residues. A peptide fragment, UQ(1-51), encompassing residues 1 to 51 of ubiquitin was produced in order to test whether this portion has propensity for independent self-assembly. Surprisingly, the construct formed a folded symmetrical dimer that was stabilised by 0.8 M sodium sulphate at 298 K (the S state). The solution structure of the UQ(1-51) dimer was determined by multinuclear NMR spectroscopy. Each subunit of UQ(1-51) consists of an N-terminal beta-hairpin followed by an alpha-helix and a final beta-strand, with orientations similar to intact ubiquitin. The dimer is formed by the third beta-strand of one subunit interleaving between the hairpin and third strand of the other to give a six-stranded beta-sheet, with the two alpha-helices sitting on top. The helix-helix and strand portions of the dimer interface also mimic related features in the structure of ubiquitin. The structural specificity of the UQ(1-51) peptide is tuneable: as the concentration of sodium sulphate is decreased, near-native alternative conformations are populated in slow chemical exchange. Magnetization transfer experiments were performed to characterize the various species present in 0.35 M sodium sulphate, namely the S state and two minor forms. Chemical shift differences suggest that one minor form is very similar to the S state, while the other experiences a significant conformational change in the third strand. A segmental rearrangement of the third strand in one subunit of the S state would render the dimer asymmetric, accounting for most of our results. Similar small-scale transitions in proteins are often invoked to explain solvent exchange at backbone amide proton sites that have an intermediate level of protection.
Disease
Known disease associated with this structure: Cleft palate, isolated OMIM:[191339]
About this Structure
1GJZ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure and properties of a dimeric N-terminal fragment of human ubiquitin., Bolton D, Evans PA, Stott K, Broadhurst RW, J Mol Biol. 2001 Dec 7;314(4):773-87. PMID:11733996
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