1a12
From Proteopedia
(New page: 200px<br /> <applet load="1a12" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a12, resolution 1.7Å" /> '''REGULATOR OF CHROMOS...) |
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| - | [[Image:1a12.gif|left|200px]]<br /> | + | [[Image:1a12.gif|left|200px]]<br /><applet load="1a12" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1a12" size=" | + | |
caption="1a12, resolution 1.7Å" /> | caption="1a12, resolution 1.7Å" /> | ||
'''REGULATOR OF CHROMOSOME CONDENSATION (RCC1) OF HUMAN'''<br /> | '''REGULATOR OF CHROMOSOME CONDENSATION (RCC1) OF HUMAN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The gene encoding the regulator of chromosome condensation (RCC1) was | + | The gene encoding the regulator of chromosome condensation (RCC1) was cloned by virtue of its ability to complement the temperature-sensitive phenotype of the hamster cell line tsBN2, which undergoes premature chromosome condensation or arrest in the G1 phase of the cell cycle at non-permissive temperatures. RCC1 homologues have been identified in many eukaryotes, including budding and fission yeast. Mutations in the gene affect pre-messenger RNA processing and transport, mating, initiation of mitosis and chromatin decondensation, suggesting that RCC1 is important in the control of nucleo-cytoplasmic transport and the cell cycle. Biochemically, RCC1 is a guanine-nucleotide-exchange factor for the nuclear Ras homologue Ran; it increases the dissociation of Ran-bound GDP by 10(5)-fold. It may also bind to DNAvia a protein-protein complex. Here we show that the structure of human RCC1, solved to 1.7-A resolution by X-ray crystallography, consists of a seven-bladed propeller formed from internal repeats of 51-68 residues per blade. The sequence and structure of the repeats differ from those of WD40-domain proteins, which also form seven-bladed propellers and include the beta-subunits of G proteins. The nature of the structure explains the consequences of a wide range of known mutations. The region of the protein that is involved in guanine-nucleotide exchange is located opposite the region that is thought to be involved in chromosome binding. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1A12 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:// | + | 1A12 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=1A12 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: ras-like nuclear gtp binding protein]] | [[Category: ras-like nuclear gtp binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:39:40 2008'' |
Revision as of 09:39, 21 February 2008
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REGULATOR OF CHROMOSOME CONDENSATION (RCC1) OF HUMAN
Contents |
Overview
The gene encoding the regulator of chromosome condensation (RCC1) was cloned by virtue of its ability to complement the temperature-sensitive phenotype of the hamster cell line tsBN2, which undergoes premature chromosome condensation or arrest in the G1 phase of the cell cycle at non-permissive temperatures. RCC1 homologues have been identified in many eukaryotes, including budding and fission yeast. Mutations in the gene affect pre-messenger RNA processing and transport, mating, initiation of mitosis and chromatin decondensation, suggesting that RCC1 is important in the control of nucleo-cytoplasmic transport and the cell cycle. Biochemically, RCC1 is a guanine-nucleotide-exchange factor for the nuclear Ras homologue Ran; it increases the dissociation of Ran-bound GDP by 10(5)-fold. It may also bind to DNAvia a protein-protein complex. Here we show that the structure of human RCC1, solved to 1.7-A resolution by X-ray crystallography, consists of a seven-bladed propeller formed from internal repeats of 51-68 residues per blade. The sequence and structure of the repeats differ from those of WD40-domain proteins, which also form seven-bladed propellers and include the beta-subunits of G proteins. The nature of the structure explains the consequences of a wide range of known mutations. The region of the protein that is involved in guanine-nucleotide exchange is located opposite the region that is thought to be involved in chromosome binding.
Disease
Known disease associated with this structure: Alveolar soft-part sarcoma OMIM:[606236]
About this Structure
1A12 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The 1.7 A crystal structure of the regulator of chromosome condensation (RCC1) reveals a seven-bladed propeller., Renault L, Nassar N, Vetter I, Becker J, Klebe C, Roth M, Wittinghofer A, Nature. 1998 Mar 5;392(6671):97-101. PMID:9510255
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