2ezy

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(New page: 200px<br /> <applet load="2ezy" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ezy" /> '''SOLUTION STRUCTURE OF HUMAN BARRIER-TO-AUTO...)
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'''SOLUTION STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR BAF, NMR, ENSEMBLE OF 20 SIMULATED ANNEALING STRUCTURES'''<br />
'''SOLUTION STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR BAF, NMR, ENSEMBLE OF 20 SIMULATED ANNEALING STRUCTURES'''<br />
==Overview==
==Overview==
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The solution structure of the human barrier-to-autointegration factor, BAF, a 21,000 Mr dimer, has been solved by NMR, including extensive use of, dipolar couplings which provide a priori long range structural, information. BAF is a highly evolutionarily conserved DNA binding protein, that is responsible for inhibiting autointegration of retroviral DNA, thereby promoting integration of retroviral DNA into the host chromosome., BAF is largely helical, and each subunit is composed of five helices. The, dimer is elongated in shape and the dimer interface comprises principally, hydrophobic contacts supplemented by a single salt bridge. Despite the, absence of any sequence similarity to any other known protein family, the, topology of helices 3-5 is similar to that of a number of DNA binding, proteins, with helices 4 and 5 constituting a helix-turn-helix motif. A, model for the interaction of BAF with DNA that is consistent with, structural and mutagenesis data is proposed.
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The solution structure of the human barrier-to-autointegration factor, BAF, a 21,000 Mr dimer, has been solved by NMR, including extensive use of dipolar couplings which provide a priori long range structural information. BAF is a highly evolutionarily conserved DNA binding protein that is responsible for inhibiting autointegration of retroviral DNA, thereby promoting integration of retroviral DNA into the host chromosome. BAF is largely helical, and each subunit is composed of five helices. The dimer is elongated in shape and the dimer interface comprises principally hydrophobic contacts supplemented by a single salt bridge. Despite the absence of any sequence similarity to any other known protein family, the topology of helices 3-5 is similar to that of a number of DNA binding proteins, with helices 4 and 5 constituting a helix-turn-helix motif. A model for the interaction of BAF with DNA that is consistent with structural and mutagenesis data is proposed.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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2EZY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=2EZY OCA].
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2EZY is a [http://en.wikipedia.org/wiki/Single_protein 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=2EZY OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Cai, M.]]
[[Category: Cai, M.]]
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[[Category: Clore, G.M.]]
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[[Category: Clore, G M.]]
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[[Category: Gronenborn, A.M.]]
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[[Category: Gronenborn, A M.]]
[[Category: aids]]
[[Category: aids]]
[[Category: dna-binding protein]]
[[Category: dna-binding protein]]
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[[Category: retroviruses]]
[[Category: retroviruses]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:57:47 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:16:15 2008''

Revision as of 15:16, 21 February 2008


2ezy

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SOLUTION STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR BAF, NMR, ENSEMBLE OF 20 SIMULATED ANNEALING STRUCTURES

Contents

Overview

The solution structure of the human barrier-to-autointegration factor, BAF, a 21,000 Mr dimer, has been solved by NMR, including extensive use of dipolar couplings which provide a priori long range structural information. BAF is a highly evolutionarily conserved DNA binding protein that is responsible for inhibiting autointegration of retroviral DNA, thereby promoting integration of retroviral DNA into the host chromosome. BAF is largely helical, and each subunit is composed of five helices. The dimer is elongated in shape and the dimer interface comprises principally hydrophobic contacts supplemented by a single salt bridge. Despite the absence of any sequence similarity to any other known protein family, the topology of helices 3-5 is similar to that of a number of DNA binding proteins, with helices 4 and 5 constituting a helix-turn-helix motif. A model for the interaction of BAF with DNA that is consistent with structural and mutagenesis data is proposed.

Disease

Known disease associated with this structure: Epilepsy, myoclonic, benign adult familial OMIM:[601068]

About this Structure

2EZY is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration., Cai M, Huang Y, Zheng R, Wei SQ, Ghirlando R, Lee MS, Craigie R, Gronenborn AM, Clore GM, Nat Struct Biol. 1998 Oct;5(10):903-9. PMID:9783751

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