2ns2
From Proteopedia
(New page: 200px<br /> <applet load="2ns2" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ns2, resolution 2.20Å" /> '''Crystal Structure o...) |
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| - | [[Image:2ns2.gif|left|200px]]<br /> | + | [[Image:2ns2.gif|left|200px]]<br /><applet load="2ns2" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="2ns2, resolution 2.20Å" /> | caption="2ns2, resolution 2.20Å" /> | ||
'''Crystal Structure of Spindlin1'''<br /> | '''Crystal Structure of Spindlin1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Spindlin1, a meiotic spindle-binding protein that is highly expressed in | + | Spindlin1, a meiotic spindle-binding protein that is highly expressed in ovarian cancer cells, was first identified as a gene involved in gametogenesis. It appeared to be a target for cell cycle-dependent phosphorylation and was demonstrated to disturb the cell cycle. Here we report the crystal structure of human spindlin1 to 2.2A of resolution, representing the first three-dimensional structure from the spin/ssty (Y-linked spermiogenesis-specific transcript) gene family. The refined structure, containing three repeats of five/four anti-parallel beta-strands, exhibits a novel arrangement of tandem Tudor-like domains. Two phosphate ions, chelated by Thr-95 and other residues, appear to stabilize the long loop between domains I and II, which might mediate the cell cycle regulation activity of spindlin1. Flow cytometry experiments indicate that cells expressing spindlin1 display a different cell cycle distribution in mitosis, whereas those expressing a T95A mutant, which had a great decrease in phosphorous content, have little effect on the cell cycle. We further identified associations of spindlin1 with nucleic acid to provide a biochemical basis for its cell cycle regulation and other functions. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2NS2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2NS2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NS2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: repeat domains]] | [[Category: repeat domains]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:10:16 2008'' |
Revision as of 16:10, 21 February 2008
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Crystal Structure of Spindlin1
Contents |
Overview
Spindlin1, a meiotic spindle-binding protein that is highly expressed in ovarian cancer cells, was first identified as a gene involved in gametogenesis. It appeared to be a target for cell cycle-dependent phosphorylation and was demonstrated to disturb the cell cycle. Here we report the crystal structure of human spindlin1 to 2.2A of resolution, representing the first three-dimensional structure from the spin/ssty (Y-linked spermiogenesis-specific transcript) gene family. The refined structure, containing three repeats of five/four anti-parallel beta-strands, exhibits a novel arrangement of tandem Tudor-like domains. Two phosphate ions, chelated by Thr-95 and other residues, appear to stabilize the long loop between domains I and II, which might mediate the cell cycle regulation activity of spindlin1. Flow cytometry experiments indicate that cells expressing spindlin1 display a different cell cycle distribution in mitosis, whereas those expressing a T95A mutant, which had a great decrease in phosphorous content, have little effect on the cell cycle. We further identified associations of spindlin1 with nucleic acid to provide a biochemical basis for its cell cycle regulation and other functions.
Disease
Known diseases associated with this structure: Dent syndrome OMIM:[300535], Fibrocalculous pancreatic diabetes, susceptibility to OMIM:[167790], Lowe syndrome OMIM:[300535], Pancreatitis, hereditary OMIM:[167790], Tropical calcific pancreatitis OMIM:[167790]
About this Structure
2NS2 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Structure of human spindlin1. Tandem tudor-like domains for cell cycle regulation., Zhao Q, Qin L, Jiang F, Wu B, Yue W, Xu F, Rong Z, Yuan H, Xie X, Gao Y, Bai C, Bartlam M, Pei X, Rao Z, J Biol Chem. 2007 Jan 5;282(1):647-56. Epub 2006 Nov 1. PMID:17082182
Page seeded by OCA on Thu Feb 21 18:10:16 2008
Categories: Homo sapiens | Single protein | Bai, C. | Bartlam, M. | Gao, Y. | Jiang, F. | Qin, L. | Rong, Z. | Wu, B. | Xie, X. | Xu, F. | Yuan, H. | Yue, W. | Zhao, Q. | PO4 | Beta barrel | Repeat domains
