1u5o

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(New page: 200px<br /><applet load="1u5o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u5o, resolution 2.50&Aring;" /> '''Structure of the D23...)
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[[Image:1u5o.jpg|left|200px]]<br /><applet load="1u5o" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1u5o.jpg|left|200px]]<br /><applet load="1u5o" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1u5o, resolution 2.50&Aring;" />
caption="1u5o, resolution 2.50&Aring;" />
'''Structure of the D23A mutant of the nuclear transport carrier NTF2'''<br />
'''Structure of the D23A mutant of the nuclear transport carrier NTF2'''<br />
==Overview==
==Overview==
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Nuclear transport carriers interact with proteins of the nuclear pore, complex (NPC) to transport their cargo across the nuclear envelope. One, such carrier is nuclear transport factor 2 (NTF2), whose import cargo is, the small GTPase Ran. A domain highly homologous to the small NTF2 protein, (14kDa) is also found in a number of additional proteins, which together, make up the NTF2 domain containing superfamily of proteins. Using, structural, computational and biochemical analysis we have identified a, functional site that is present throughout this superfamily, and our, results indicate that this site functions as an NPC binding site in NTF2., Previously we showed that a D23A mutant of NTF2 exhibits increased, affinity for the NPC. The mechanism of this mutation, however, was unknown, as this region of NTF2 had not been implicated in binding to NPC proteins., Here we show that the D23A mutation in NTF2 does not result in gross, structural changes affecting other known NPC binding sites. Instead, the, D23 residue is located in an evolutionarily important region in the NTF2, domain containing superfamily, that in NTF2, is involved in binding to the, NPC.
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Nuclear transport carriers interact with proteins of the nuclear pore complex (NPC) to transport their cargo across the nuclear envelope. One such carrier is nuclear transport factor 2 (NTF2), whose import cargo is the small GTPase Ran. A domain highly homologous to the small NTF2 protein (14kDa) is also found in a number of additional proteins, which together make up the NTF2 domain containing superfamily of proteins. Using structural, computational and biochemical analysis we have identified a functional site that is present throughout this superfamily, and our results indicate that this site functions as an NPC binding site in NTF2. Previously we showed that a D23A mutant of NTF2 exhibits increased affinity for the NPC. The mechanism of this mutation, however, was unknown as this region of NTF2 had not been implicated in binding to NPC proteins. Here we show that the D23A mutation in NTF2 does not result in gross structural changes affecting other known NPC binding sites. Instead, the D23 residue is located in an evolutionarily important region in the NTF2 domain containing superfamily, that in NTF2, is involved in binding to the NPC.
==About this Structure==
==About this Structure==
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1U5O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U5O OCA].
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1U5O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U5O OCA].
==Reference==
==Reference==
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bowman, B.R.]]
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[[Category: Bowman, B R.]]
[[Category: Cushman, I.]]
[[Category: Cushman, I.]]
[[Category: Lichtarge, O.]]
[[Category: Lichtarge, O.]]
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[[Category: Moore, M.S.]]
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[[Category: Moore, M S.]]
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[[Category: Quiocho, F.A.]]
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[[Category: Quiocho, F A.]]
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[[Category: Sowa, M.E.]]
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[[Category: Sowa, M E.]]
[[Category: ntf2 mutant d23a]]
[[Category: ntf2 mutant d23a]]
[[Category: nuclear transport protein]]
[[Category: nuclear transport protein]]
[[Category: transport]]
[[Category: transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:51:40 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:20:55 2008''

Revision as of 13:20, 21 February 2008


1u5o, resolution 2.50Å

Drag the structure with the mouse to rotate

Structure of the D23A mutant of the nuclear transport carrier NTF2

Overview

Nuclear transport carriers interact with proteins of the nuclear pore complex (NPC) to transport their cargo across the nuclear envelope. One such carrier is nuclear transport factor 2 (NTF2), whose import cargo is the small GTPase Ran. A domain highly homologous to the small NTF2 protein (14kDa) is also found in a number of additional proteins, which together make up the NTF2 domain containing superfamily of proteins. Using structural, computational and biochemical analysis we have identified a functional site that is present throughout this superfamily, and our results indicate that this site functions as an NPC binding site in NTF2. Previously we showed that a D23A mutant of NTF2 exhibits increased affinity for the NPC. The mechanism of this mutation, however, was unknown as this region of NTF2 had not been implicated in binding to NPC proteins. Here we show that the D23A mutation in NTF2 does not result in gross structural changes affecting other known NPC binding sites. Instead, the D23 residue is located in an evolutionarily important region in the NTF2 domain containing superfamily, that in NTF2, is involved in binding to the NPC.

About this Structure

1U5O is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Computational and biochemical identification of a nuclear pore complex binding site on the nuclear transport carrier NTF2., Cushman I, Bowman BR, Sowa ME, Lichtarge O, Quiocho FA, Moore MS, J Mol Biol. 2004 Nov 19;344(2):303-10. PMID:15522285

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