1vg9: Difference between revisions
New page: left|200px<br /><applet load="1vg9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vg9, resolution 2.50Å" /> '''The crystal structur... |
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[[Image:1vg9.jpg|left|200px]]<br /><applet load="1vg9" size=" | [[Image:1vg9.jpg|left|200px]]<br /><applet load="1vg9" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1vg9, resolution 2.50Å" /> | caption="1vg9, resolution 2.50Å" /> | ||
'''The crystal structures of the REP-1 protein in complex with C-terminally truncated Rab7 protein'''<br /> | '''The crystal structures of the REP-1 protein in complex with C-terminally truncated Rab7 protein'''<br /> | ||
==Overview== | ==Overview== | ||
Members of the RabGDI/REP family serve as multifunctional regulators of | Members of the RabGDI/REP family serve as multifunctional regulators of the Rab family of GTP binding proteins. Mutations in members of this family, such as REP-1, lead to abnormalities, including progressive retinal degradation (choroideremia) in humans. The crystal structures of the REP-1 protein in complex with monoprenylated or C-terminally truncated Rab7 proteins revealed that Rab7 interacts with the Rab binding platform of REP-1 via an extended interface involving the Switch 1 and 2 regions. The C terminus of the REP-1 molecule functions as a mobile lid covering a conserved hydrophobic patch on the surface of REP-1 that in the complex coordinates the C terminus of Rab proteins. Using semisynthetic fluorescent Rab27A, we demonstrate that although Rab27A can be prenylated by REP-2, this reaction can be effectively inhibited by other Rab proteins, providing a possible explanation for the accumulation of unprenylated Rab27A in choroideremia. | ||
==About this Structure== | ==About this Structure== | ||
1VG9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with MG, K, GDP and P33 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1VG9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=GDP:'>GDP</scene> and <scene name='pdbligand=P33:'>P33</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VG9 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Alexandrov, K.]] | [[Category: Alexandrov, K.]] | ||
[[Category: Goody, R | [[Category: Goody, R S.]] | ||
[[Category: Niculae, A.]] | [[Category: Niculae, A.]] | ||
[[Category: Pyatkov, K.]] | [[Category: Pyatkov, K.]] | ||
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[[Category: rab prenylation]] | [[Category: rab prenylation]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:35:00 2008'' | ||
Revision as of 13:35, 21 February 2008
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The crystal structures of the REP-1 protein in complex with C-terminally truncated Rab7 protein
Overview
Members of the RabGDI/REP family serve as multifunctional regulators of the Rab family of GTP binding proteins. Mutations in members of this family, such as REP-1, lead to abnormalities, including progressive retinal degradation (choroideremia) in humans. The crystal structures of the REP-1 protein in complex with monoprenylated or C-terminally truncated Rab7 proteins revealed that Rab7 interacts with the Rab binding platform of REP-1 via an extended interface involving the Switch 1 and 2 regions. The C terminus of the REP-1 molecule functions as a mobile lid covering a conserved hydrophobic patch on the surface of REP-1 that in the complex coordinates the C terminus of Rab proteins. Using semisynthetic fluorescent Rab27A, we demonstrate that although Rab27A can be prenylated by REP-2, this reaction can be effectively inhibited by other Rab proteins, providing a possible explanation for the accumulation of unprenylated Rab27A in choroideremia.
About this Structure
1VG9 is a Protein complex structure of sequences from Rattus norvegicus with MG, K, GDP and P33 as ligands. Full crystallographic information is available from OCA.
Reference
Structure of the Rab7:REP-1 complex: insights into the mechanism of Rab prenylation and choroideremia disease., Rak A, Pylypenko O, Niculae A, Pyatkov K, Goody RS, Alexandrov K, Cell. 2004 Jun 11;117(6):749-60. PMID:15186776
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