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New page: left|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 />
<applet load="1a12" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1a12, resolution 1.7&Aring;" />
'''REGULATOR OF CHROMOSOME CONDENSATION (RCC1) OF HUMAN'''<br />


==Overview==
==REGULATOR OF CHROMOSOME CONDENSATION (RCC1) OF HUMAN==
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.
<StructureSection load='1a12' size='340' side='right'caption='[[1a12]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 
== Structural highlights ==
==Disease==
<table><tr><td colspan='2'>[[1a12]] is a 3 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A12 FirstGlance]. <br>
Known disease associated with this structure: Alveolar soft-part sarcoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=606236 606236]]
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
 
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a12 OCA], [https://pdbe.org/1a12 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a12 RCSB], [https://www.ebi.ac.uk/pdbsum/1a12 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a12 ProSAT]</span></td></tr>
==About this Structure==
</table>
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A12 OCA].
== Function ==
 
[https://www.uniprot.org/uniprot/RCC1_HUMAN RCC1_HUMAN] Guanine-nucleotide releasing factor that promotes the exchange of Ran-bound GDP by GTP. Involved in the regulation of onset of chromosome condensation in the S phase. Binds both to the nucleosomes and double-stranded DNA. RCC1-Ran complex (together with other proteins) acts as a component of a signal transmission pathway that detects unreplicated DNA. Plays a key role in nucleo-cytoplasmic transport, mitosis and nuclear-envelope assembly.<ref>PMID:1944575</ref>
==Reference==
== Evolutionary Conservation ==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9510255 9510255]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a1/1a12_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a12 ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Becker, J.]]
[[Category: Becker J]]
[[Category: Nassar, N.]]
[[Category: Nassar N]]
[[Category: Renault, L.]]
[[Category: Renault L]]
[[Category: Roth, M.]]
[[Category: Roth M]]
[[Category: Vetter, I.]]
[[Category: Vetter I]]
[[Category: Wittinghofer, A.]]
[[Category: Wittinghofer A]]
[[Category: gef]]
[[Category: guanine nucleotide exchange factor]]
[[Category: ran]]
[[Category: ras-like nuclear gtp binding protein]]
 
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Latest revision as of 06:26, 7 February 2024

REGULATOR OF CHROMOSOME CONDENSATION (RCC1) OF HUMAN

1a12, resolution 1.70Å

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