2eho

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(New page: 200px<br /> <applet load="2eho" size="450" color="white" frame="true" align="right" spinBox="true" caption="2eho, resolution 3.00&Aring;" /> '''Crystal structure o...)
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[[Image:2eho.gif|left|200px]]<br />
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[[Image:2eho.jpg|left|200px]]<br /><applet load="2eho" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="2eho" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2eho, resolution 3.00&Aring;" />
caption="2eho, resolution 3.00&Aring;" />
'''Crystal structure of human GINS complex'''<br />
'''Crystal structure of human GINS complex'''<br />
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==Overview==
==Overview==
The GINS complex mediates the assembly of the MCM2-7 (minichromosome, maintenance) complex with proteins in a replisome progression complex. The, eukaryotic GINS complex is composed of Sld5, Psf1, Psf2, and Psf3, which, must be assembled for cell proliferation. We determined the crystal, structure of the human GINS complex: GINS forms an elliptical shape with a, small central channel. The structures of Sld5 and Psf2 resemble those of, Psf1 and Psf3, respectively. In addition, the N-terminal and C-terminal, domains of Sld5/Psf1 are permuted in Psf2/Psf3, which suggests that the, four proteins have evolved from a common ancestor. Using a structure-based, mutational analysis, we identified the functionally critical surface, regions of the GINS complex.
The GINS complex mediates the assembly of the MCM2-7 (minichromosome, maintenance) complex with proteins in a replisome progression complex. The, eukaryotic GINS complex is composed of Sld5, Psf1, Psf2, and Psf3, which, must be assembled for cell proliferation. We determined the crystal, structure of the human GINS complex: GINS forms an elliptical shape with a, small central channel. The structures of Sld5 and Psf2 resemble those of, Psf1 and Psf3, respectively. In addition, the N-terminal and C-terminal, domains of Sld5/Psf1 are permuted in Psf2/Psf3, which suggests that the, four proteins have evolved from a common ancestor. Using a structure-based, mutational analysis, we identified the functionally critical surface, regions of the GINS complex.
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==Disease==
 
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Known diseases associated with this structure: Bare lymphocyte syndrome, type I OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=170260 170260]], Bare lymphocyte syndrome, type I, due to TAP2 deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=170261 170261]], Wegener-like granulomatosis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=170261 170261]]
 
==About this Structure==
==About this Structure==
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2EHO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2EHO OCA].
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2EHO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EHO OCA].
==Reference==
==Reference==
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[[Category: protein-protein complex]]
[[Category: protein-protein complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:50:06 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:48:36 2008''

Revision as of 12:48, 23 January 2008


2eho, resolution 3.00Å

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Crystal structure of human GINS complex

Overview

The GINS complex mediates the assembly of the MCM2-7 (minichromosome, maintenance) complex with proteins in a replisome progression complex. The, eukaryotic GINS complex is composed of Sld5, Psf1, Psf2, and Psf3, which, must be assembled for cell proliferation. We determined the crystal, structure of the human GINS complex: GINS forms an elliptical shape with a, small central channel. The structures of Sld5 and Psf2 resemble those of, Psf1 and Psf3, respectively. In addition, the N-terminal and C-terminal, domains of Sld5/Psf1 are permuted in Psf2/Psf3, which suggests that the, four proteins have evolved from a common ancestor. Using a structure-based, mutational analysis, we identified the functionally critical surface, regions of the GINS complex.

About this Structure

2EHO is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the human GINS complex., Choi JM, Lim HS, Kim JJ, Song OK, Cho Y, Genes Dev. 2007 Jun 1;21(11):1316-21. PMID:17545466

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