2ns2
From Proteopedia
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|PDB= 2ns2 |SIZE=350|CAPTION= <scene name='initialview01'>2ns2</scene>, resolution 2.20Å | |PDB= 2ns2 |SIZE=350|CAPTION= <scene name='initialview01'>2ns2</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= SPIN, OCR, SPIN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= SPIN, OCR, SPIN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ns2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ns2 OCA], [http://www.ebi.ac.uk/pdbsum/2ns2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ns2 RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Dent syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=300535 300535]], Fibrocalculous pancreatic diabetes, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=167790 167790]], Lowe syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=300535 300535]], Pancreatitis, hereditary OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=167790 167790]], Tropical calcific pancreatitis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=167790 167790]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Yue, W.]] | [[Category: Yue, W.]] | ||
[[Category: Zhao, Q.]] | [[Category: Zhao, Q.]] | ||
| - | [[Category: PO4]] | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
[[Category: repeat domain]] | [[Category: repeat domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:07:27 2008'' |
Revision as of 01:07, 31 March 2008
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| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | SPIN, OCR, SPIN1 (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Spindlin1
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.
About this Structure
2NS2 is a Single protein structure of sequence from Homo sapiens. 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 Mon Mar 31 04:07:27 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. | Beta barrel | Repeat domain
