This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1jxs

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Solution Structure of the DNA-Binding Domain of Interleukin Enhancer Binding Factor

Structural highlights

1jxs is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FOXK2_HUMAN Recognizes the core sequence 5'-TAAACA-3'. Binds to NFAT-like motifs (purine-rich) in the IL2 promoter. Also binds to HIV-1 long terminal repeat. May be involved in both positive and negative regulation of important viral and cellular promoter elements.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Interleukin enhancer binding factor (ILF) binds to the interleukin-2 (IL-2) promoter and regulates IL-2 gene expression. In this study, the 3D structure of the DNA-binding domain of ILF was determined by multidimensional NMR spectroscopy. NMR structure analysis revealed that the DNA-binding domain of ILF is a new member of the winged helix/forkhead family, and that its wing 2 contains an extra alpha-helix. This is the first study to report the presence of a C-terminal alpha-helix in place of a typical wing 2 in a member of this family. This structural difference may be responsible for the different DNA-binding specificity of ILF compared to other winged helix/forkhead proteins. Our deletion studies of the fragments of ILF also suggest that the C-terminal region plays a regulatory role in DNA binding.

Solution structure of the DNA-binding domain of interleukin enhancer binding factor 1 (FOXK1a).,Liu PP, Chen YC, Li C, Hsieh YH, Chen SW, Chen SH, Jeng WY, Chuang WJ Proteins. 2002 Dec 1;49(4):543-53. PMID:12402362^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Li C, Lai CF, Sigman DS, Gaynor RB. Cloning of a cellular factor, interleukin binding factor, that binds to NFAT-like motifs in the human immunodeficiency virus long terminal repeat. Proc Natl Acad Sci U S A. 1991 Sep 1;88(17):7739-43. PMID:1909027
↑ Li C, Lusis AJ, Sparkes R, Nirula A, Gaynor R. Characterization and chromosomal mapping of the gene encoding the cellular DNA binding protein ILF. Genomics. 1992 Jul;13(3):665-71. PMID:1339390
↑ Liu PP, Chen YC, Li C, Hsieh YH, Chen SW, Chen SH, Jeng WY, Chuang WJ. Solution structure of the DNA-binding domain of interleukin enhancer binding factor 1 (FOXK1a). Proteins. 2002 Dec 1;49(4):543-53. PMID:12402362 doi:10.1002/prot.10227

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1jxs"

@@ Line 19: / Line 19: @@
 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jxs ConSurf].
 <div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Interleukin enhancer binding factor (ILF) binds to the interleukin-2 (IL-2) promoter and regulates IL-2 gene expression. In this study, the 3D structure of the DNA-binding domain of ILF was determined by multidimensional NMR spectroscopy. NMR structure analysis revealed that the DNA-binding domain of ILF is a new member of the winged helix/forkhead family, and that its wing 2 contains an extra alpha-helix. This is the first study to report the presence of a C-terminal alpha-helix in place of a typical wing 2 in a member of this family. This structural difference may be responsible for the different DNA-binding specificity of ILF compared to other winged helix/forkhead proteins. Our deletion studies of the fragments of ILF also suggest that the C-terminal region plays a regulatory role in DNA binding.
+Solution structure of the DNA-binding domain of interleukin enhancer binding factor 1 (FOXK1a).,Liu PP, Chen YC, Li C, Hsieh YH, Chen SW, Chen SH, Jeng WY, Chuang WJ Proteins. 2002 Dec 1;49(4):543-53. PMID:12402362<ref>PMID:12402362</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1jxs" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

1jxs

From Proteopedia

Current revision

Solution Structure of the DNA-Binding Domain of Interleukin Enhancer Binding Factor

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox