From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:2pi2.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2pi2.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_2pi2| PDB=2pi2 | SCENE= }} | | {{STRUCTURE_2pi2| PDB=2pi2 | SCENE= }} |
| | | | |
| - | '''Full-length Replication protein A subunits RPA14 and RPA32'''
| + | ===Full-length Replication protein A subunits RPA14 and RPA32=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | Replication protein A (RPA) is the ubiquitous, eukaryotic single-stranded DNA (ssDNA) binding protein and is essential for DNA replication, recombination, and repair. Here, crystal structures of the soluble RPA heterodimer, composed of the RPA14 and RPA32 subunits, have been determined for the full-length protein in multiple crystal forms. In all crystals, the electron density for the N-terminal (residues 1-42) and C-terminal (residues 175-270) regions of RPA32 is weak and of poor quality indicating that these regions are disordered and/or assume multiple positions in the crystals. Hence, the RPA32 N terminus, that is hyperphosphorylated in a cell-cycle-dependent manner and in response to DNA damaging agents, appears to be inherently disordered in the unphosphorylated state. The C-terminal, winged helix-loop-helix, protein-protein interaction domain adopts several conformations perhaps to facilitate its interaction with various proteins. Although the ordered regions of RPA14/32 resemble the previously solved protease-resistant core crystal structure, the quaternary structures between the heterodimers are quite different. Thus, the four-helix bundle quaternary assembly noted in the original core structure is unlikely to be related to the quaternary structure of the intact heterotrimer. An organic ligand binding site between subunits RPA14 and RPA32 was identified to bind dioxane. Comparison of the ssDNA binding surfaces of RPA70 with RPA14/32 showed that the lower affinity of RPA14/32 can be attributed to a shallower binding crevice with reduced positive electrostatic charge.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17976647}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17976647 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_17976647}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 30: |
Line 34: |
| | [[Category: Replication]] | | [[Category: Replication]] |
| | [[Category: Ssdna binding protein]] | | [[Category: Ssdna binding protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:09:06 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:24:55 2008'' |
Revision as of 04:25, 29 July 2008
Template:STRUCTURE 2pi2
Full-length Replication protein A subunits RPA14 and RPA32
Template:ABSTRACT PUBMED 17976647
About this Structure
2PI2 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the full-length human RPA14/32 complex gives insights into the mechanism of DNA binding and complex formation., Deng X, Habel JE, Kabaleeswaran V, Snell EH, Wold MS, Borgstahl GE, J Mol Biol. 2007 Dec 7;374(4):865-76. Epub 2007 Oct 2. PMID:17976647
Page seeded by OCA on Tue Jul 29 07:24:55 2008
