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1rrp
From Proteopedia
(New page: 200px<br /> <applet load="1rrp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rrp, resolution 2.96Å" /> '''STRUCTURE OF THE RA...) |
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| - | [[Image:1rrp. | + | [[Image:1rrp.jpg|left|200px]]<br /><applet load="1rrp" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1rrp" size=" | + | |
caption="1rrp, resolution 2.96Å" /> | caption="1rrp, resolution 2.96Å" /> | ||
'''STRUCTURE OF THE RAN-GPPNHP-RANBD1 COMPLEX'''<br /> | '''STRUCTURE OF THE RAN-GPPNHP-RANBD1 COMPLEX'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1RRP 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 MG and GNP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1RRP 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=MG:'>MG</scene> and <scene name='pdbligand=GNP:'>GNP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RRP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: small gtpase]] | [[Category: small gtpase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:49:28 2008'' |
Revision as of 14:49, 15 February 2008
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STRUCTURE OF THE RAN-GPPNHP-RANBD1 COMPLEX
Contents |
Overview
The protein Ran is a small GTP-binding protein that binds to two types of, effector inside the cell: Ran-binding proteins, which have a role in, terminating export processes from the nucleus to the cytoplasm, and, importin-beta-like molecules that bind cargo proteins during nuclear, transport. The Ran-binding domain is a conserved sequence motif found in, several proteins that participate in these transport processes. The, Ran-binding protein RanBP2 contains four of these domains and constitutes, a large part of the cytoplasmic fibrils that extend from the nuclear-pore, complex. The structure of Ran bound to a non-hydrolysable GTP analogue, (Ran x GppNHp) in complex with the first Ran-binding domain (RanBD1) of, human RanBP2 reveals not only that RanBD1 has a pleckstrin-homology domain, fold, but also that the switch-I region of Ran x GppNHp resembles the, canonical Ras GppNHp structure and that the carboxy terminus of Ran is, wrapped around RanBD1, contacting a basic patch on RanBD1 through its, acidic end. This molecular 'embrace' enables RanBDs to sequester the Ran, carboxy terminus, triggering the dissociation of Ran x GTP from, importin-beta-related transport factors and facilitating GTP hydrolysis by, the GTPase-activating protein ranGAP. Such a mechanism represents a new, type of switch mechanism and regulatory protein-protein interaction for a, Ras-related protein.
Disease
Known diseases associated with this structure: Osteolysis, familial expansile OMIM:[603499], Paget disease of bone OMIM:[603499]
About this Structure
1RRP is a Protein complex structure of sequences from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport., Vetter IR, Nowak C, Nishimoto T, Kuhlmann J, Wittinghofer A, Nature. 1999 Mar 4;398(6722):39-46. PMID:10078529
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