This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2d68
From Proteopedia
(New page: 200px<br /> <applet load="2d68" size="450" color="white" frame="true" align="right" spinBox="true" caption="2d68, resolution 1.60Å" /> '''Structure of the N-...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2d68.gif|left|200px]]<br /> | + | [[Image:2d68.gif|left|200px]]<br /><applet load="2d68" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2d68" size=" | + | |
caption="2d68, resolution 1.60Å" /> | caption="2d68, resolution 1.60Å" /> | ||
'''Structure of the N-terminal domain of FOP (FGFR1OP) protein'''<br /> | '''Structure of the N-terminal domain of FOP (FGFR1OP) protein'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The fibroblast growth factor receptor 1 (FGFR1) oncogene partner, FOP, is | + | The fibroblast growth factor receptor 1 (FGFR1) oncogene partner, FOP, is a centrosomal protein that is involved in the anchoring of microtubules (MTS) to subcellular structures. The protein was originally discovered as a fusion partner with FGFR1 in oncoproteins that give rise to stem cell myeloproliferative disorders. A subsequent proteomics screen identified FOP as a component of the centrosome. FOP contains a Lis-homology (LisH) motif found in more than 100 eukaryotic proteins. LisH motifs are believed to be involved in microtubule dynamics and organization, cell migration, and chromosome segregation; several of them are associated with genetic diseases. We report here a 1.6A resolution crystal structure of the N-terminal dimerization domain of FOP. The structure comprises an alpha-helical bundle composed of two antiparallel chains, each of them having five alpha-helices. The central part of the dimer contains the LisH domain. We further determined that the FOP LisH domain is part of a longer N-terminal segment that is required, albeit not sufficient, for dimerization and centrosomal localization of FOP. |
==Disease== | ==Disease== | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2D68 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:// | + | 2D68 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=2D68 OCA]. |
==Reference== | ==Reference== | ||
| Line 21: | Line 20: | ||
[[Category: dimer]] | [[Category: dimer]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:55:46 2008'' |
Revision as of 14:55, 21 February 2008
|
Structure of the N-terminal domain of FOP (FGFR1OP) protein
Contents |
Overview
The fibroblast growth factor receptor 1 (FGFR1) oncogene partner, FOP, is a centrosomal protein that is involved in the anchoring of microtubules (MTS) to subcellular structures. The protein was originally discovered as a fusion partner with FGFR1 in oncoproteins that give rise to stem cell myeloproliferative disorders. A subsequent proteomics screen identified FOP as a component of the centrosome. FOP contains a Lis-homology (LisH) motif found in more than 100 eukaryotic proteins. LisH motifs are believed to be involved in microtubule dynamics and organization, cell migration, and chromosome segregation; several of them are associated with genetic diseases. We report here a 1.6A resolution crystal structure of the N-terminal dimerization domain of FOP. The structure comprises an alpha-helical bundle composed of two antiparallel chains, each of them having five alpha-helices. The central part of the dimer contains the LisH domain. We further determined that the FOP LisH domain is part of a longer N-terminal segment that is required, albeit not sufficient, for dimerization and centrosomal localization of FOP.
Disease
Known diseases associated with this structure: Fibrodysplasia ossificans progressiva OMIM:[102576], Myeloproliferative disorder OMIM:[605392]
About this Structure
2D68 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the N-terminal domain of the FOP (FGFR1OP) protein and implications for its dimerization and centrosomal localization., Mikolajka A, Yan X, Popowicz GM, Smialowski P, Nigg EA, Holak TA, J Mol Biol. 2006 Jun 16;359(4):863-75. Epub 2006 Apr 24. PMID:16690081
Page seeded by OCA on Thu Feb 21 16:55:46 2008
