2p2r

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==Overview==
==Overview==
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KH (hnRNP K homology) domains, consisting of approximately 70 amino acid, residues, are present in a variety of nucleic-acid-binding proteins. Among, these are poly(C)-binding proteins (PCBPs), which are important regulators, of mRNA stability and posttranscriptional regulation in general. All PCBPs, contain three different KH domains and recognize poly(C)-sequences with, high affinity and specificity. To reveal the molecular basis of, poly(C)-sequence recognition, we have determined the crystal structure, at, 1.6 A resolution, of PCBP2 KH3 domain in complex with a 7-nt DNA sequence, (5'-AACCCTA-3') corresponding to one repeat of the C-rich strand of human, telomeric DNA. The domain assumes a type-I KH fold in a, betaalphaalphabetabetaalpha configuration. The protein-DNA interface could, be studied in unprecedented detail and is made up of a series of direct, and water-mediated hydrogen bonds between the protein and the DNA, revealing an especially dense network involving several structural water, molecules for the last 2 nt in the core recognition sequence. Unlike, published KH domain structures, the protein crystallizes without, protein-protein contacts, yielding new insights into the dimerization, properties of different KH domains. A nucleotide platform, an interesting, feature found in some RNA molecules, was identified, evidently for the, first time in DNA.
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KH (hnRNP K homology) domains, consisting of approximately 70 amino acid residues, are present in a variety of nucleic-acid-binding proteins. Among these are poly(C)-binding proteins (PCBPs), which are important regulators of mRNA stability and posttranscriptional regulation in general. All PCBPs contain three different KH domains and recognize poly(C)-sequences with high affinity and specificity. To reveal the molecular basis of poly(C)-sequence recognition, we have determined the crystal structure, at 1.6 A resolution, of PCBP2 KH3 domain in complex with a 7-nt DNA sequence (5'-AACCCTA-3') corresponding to one repeat of the C-rich strand of human telomeric DNA. The domain assumes a type-I KH fold in a betaalphaalphabetabetaalpha configuration. The protein-DNA interface could be studied in unprecedented detail and is made up of a series of direct and water-mediated hydrogen bonds between the protein and the DNA, revealing an especially dense network involving several structural water molecules for the last 2 nt in the core recognition sequence. Unlike published KH domain structures, the protein crystallizes without protein-protein contacts, yielding new insights into the dimerization properties of different KH domains. A nucleotide platform, an interesting feature found in some RNA molecules, was identified, evidently for the first time in DNA.
==About this Structure==
==About this Structure==
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[[Category: Du, Z.]]
[[Category: Du, Z.]]
[[Category: Fenn, S.]]
[[Category: Fenn, S.]]
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[[Category: James, T.L.]]
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[[Category: James, T L.]]
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[[Category: Lee, J.K.]]
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[[Category: Lee, J K.]]
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[[Category: Stroud, R.M.]]
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[[Category: Stroud, R M.]]
[[Category: Tjhen, R.]]
[[Category: Tjhen, R.]]
[[Category: CYT]]
[[Category: CYT]]
[[Category: protein-dna complex]]
[[Category: protein-dna complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:55:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:25:14 2008''

Revision as of 16:25, 21 February 2008

Image:2p2r.gif

2p2r, resolution 1.60Å

Drag the structure with the mouse to rotate

Crystal structure of the third KH domain of human Poly(C)-Binding Protein-2 in complex with C-rich strand of human telomeric DNA

Overview

KH (hnRNP K homology) domains, consisting of approximately 70 amino acid residues, are present in a variety of nucleic-acid-binding proteins. Among these are poly(C)-binding proteins (PCBPs), which are important regulators of mRNA stability and posttranscriptional regulation in general. All PCBPs contain three different KH domains and recognize poly(C)-sequences with high affinity and specificity. To reveal the molecular basis of poly(C)-sequence recognition, we have determined the crystal structure, at 1.6 A resolution, of PCBP2 KH3 domain in complex with a 7-nt DNA sequence (5'-AACCCTA-3') corresponding to one repeat of the C-rich strand of human telomeric DNA. The domain assumes a type-I KH fold in a betaalphaalphabetabetaalpha configuration. The protein-DNA interface could be studied in unprecedented detail and is made up of a series of direct and water-mediated hydrogen bonds between the protein and the DNA, revealing an especially dense network involving several structural water molecules for the last 2 nt in the core recognition sequence. Unlike published KH domain structures, the protein crystallizes without protein-protein contacts, yielding new insights into the dimerization properties of different KH domains. A nucleotide platform, an interesting feature found in some RNA molecules, was identified, evidently for the first time in DNA.

About this Structure

2P2R is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the third KH domain of human poly(C)-binding protein-2 in complex with a C-rich strand of human telomeric DNA at 1.6 A resolution., Fenn S, Du Z, Lee JK, Tjhen R, Stroud RM, James TL, Nucleic Acids Res. 2007;35(8):2651-60. Epub 2007 Apr 10. PMID:17426136

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