1cqt

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(New page: 200px<br /> <applet load="1cqt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cqt, resolution 3.20&Aring;" /> '''CRYSTAL STRUCTURE O...)
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caption="1cqt, resolution 3.20&Aring;" />
'''CRYSTAL STRUCTURE OF A TERNARY COMPLEX CONTAINING AN OCA-B PEPTIDE, THE OCT-1 POU DOMAIN, AND AN OCTAMER ELEMENT'''<br />
'''CRYSTAL STRUCTURE OF A TERNARY COMPLEX CONTAINING AN OCA-B PEPTIDE, THE OCT-1 POU DOMAIN, AND AN OCTAMER ELEMENT'''<br />
==Overview==
==Overview==
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We have determined the crystal structure, at 3.2 A, of a ternary complex, containing an OCA-B peptide, the Oct-1 POU domain, and an octamer DNA, site. The OCA-B peptide binds in the major groove near the center of the, octamer site, and its polypeptide backbone forms a pair of hydrogen bonds, with the adenine base at position 5 of the octamer DNA. Numerous, protein-protein contacts between the OCA-B peptide and the POU domain are, also involved in the ternary complex. In particular, the hydrophobic, surface from a short alpha-helix of OCA-B helps to stabilize the complex, by binding to a hydrophobic pocket on the POU-specific domain. The, structure of this ternary complex is consistent with previous biochemical, studies and shows how peptide-DNA and peptide-protein contacts from OCA-B, provide structural and functional specificity in the regulation of, immunoglobulin transcription.
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We have determined the crystal structure, at 3.2 A, of a ternary complex containing an OCA-B peptide, the Oct-1 POU domain, and an octamer DNA site. The OCA-B peptide binds in the major groove near the center of the octamer site, and its polypeptide backbone forms a pair of hydrogen bonds with the adenine base at position 5 of the octamer DNA. Numerous protein-protein contacts between the OCA-B peptide and the POU domain are also involved in the ternary complex. In particular, the hydrophobic surface from a short alpha-helix of OCA-B helps to stabilize the complex by binding to a hydrophobic pocket on the POU-specific domain. The structure of this ternary complex is consistent with previous biochemical studies and shows how peptide-DNA and peptide-protein contacts from OCA-B provide structural and functional specificity in the regulation of immunoglobulin transcription.
==About this Structure==
==About this Structure==
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1CQT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CQT OCA].
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1CQT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1CQT OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Cepek, K.]]
[[Category: Cepek, K.]]
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[[Category: Chasman, D.I.]]
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[[Category: Chasman, D I.]]
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[[Category: Pabo, C.O.]]
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[[Category: Pabo, C O.]]
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[[Category: Sharp, P.A.]]
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[[Category: Sharp, P A.]]
[[Category: gene regulation/dna]]
[[Category: gene regulation/dna]]
[[Category: oca-b]]
[[Category: oca-b]]
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[[Category: protein-dna interface]]
[[Category: protein-dna interface]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:24:36 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:08:46 2008''

Revision as of 10:08, 21 February 2008


1cqt, resolution 3.20Å

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CRYSTAL STRUCTURE OF A TERNARY COMPLEX CONTAINING AN OCA-B PEPTIDE, THE OCT-1 POU DOMAIN, AND AN OCTAMER ELEMENT

Overview

We have determined the crystal structure, at 3.2 A, of a ternary complex containing an OCA-B peptide, the Oct-1 POU domain, and an octamer DNA site. The OCA-B peptide binds in the major groove near the center of the octamer site, and its polypeptide backbone forms a pair of hydrogen bonds with the adenine base at position 5 of the octamer DNA. Numerous protein-protein contacts between the OCA-B peptide and the POU domain are also involved in the ternary complex. In particular, the hydrophobic surface from a short alpha-helix of OCA-B helps to stabilize the complex by binding to a hydrophobic pocket on the POU-specific domain. The structure of this ternary complex is consistent with previous biochemical studies and shows how peptide-DNA and peptide-protein contacts from OCA-B provide structural and functional specificity in the regulation of immunoglobulin transcription.

About this Structure

1CQT is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of an OCA-B peptide bound to an Oct-1 POU domain/octamer DNA complex: specific recognition of a protein-DNA interface., Chasman D, Cepek K, Sharp PA, Pabo CO, Genes Dev. 1999 Oct 15;13(20):2650-7. PMID:10541551

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