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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/Q8U0X6_PYRFU Q8U0X6_PYRFU] | | [https://www.uniprot.org/uniprot/Q8U0X6_PYRFU Q8U0X6_PYRFU] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Targeting of proteins for structure determination in structural genomic programs often includes the use of threading and fold recognition methods to exclude proteins belonging to well-populated fold families, but such methods can still fail to recognize preexisting folds. The authors illustrate here a method in which limited amounts of structural data are used to improve an initial homology search and the data are subsequently used to produce a structure by data-constrained refinement of an identified structural template. The data used are primarily NMR-based residual dipolar couplings, but they also include additional chemical shift and backbone-nuclear Overhauser effect data. Using this methodology, a backbone structure was efficiently produced for a 10 kDa protein (PF1455) from Pyrococcus furiosus. Its relationship to existing structures and its probable function are discussed.
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| Structure determination of a new protein from backbone-centered NMR data and NMR-assisted structure prediction.,Mayer KL, Qu Y, Bansal S, LeBlond PD, Jenney FE Jr, Brereton PS, Adams MW, Xu Y, Prestegard JH Proteins. 2006 Nov 1;65(2):480-9. PMID:16927360<ref>PMID:16927360</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 2f40" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
