1ewi: Difference between revisions
New page: left|200px<br /> <applet load="1ewi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ewi" /> '''HUMAN REPLICATION PROTEIN A: GLOBAL FOLD OF... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1ewi.gif|left|200px]]<br /> | [[Image:1ewi.gif|left|200px]]<br /><applet load="1ewi" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1ewi" size=" | |||
caption="1ewi" /> | caption="1ewi" /> | ||
'''HUMAN REPLICATION PROTEIN A: GLOBAL FOLD OF THE N-TERMINAL RPA-70 DOMAIN REVEALS A BASIC CLEFT AND FLEXIBLE C-TERMINAL LINKER'''<br /> | '''HUMAN REPLICATION PROTEIN A: GLOBAL FOLD OF THE N-TERMINAL RPA-70 DOMAIN REVEALS A BASIC CLEFT AND FLEXIBLE C-TERMINAL LINKER'''<br /> | ||
==Overview== | ==Overview== | ||
Human Replication Protein A (hsRPA) is required for multiple cellular | Human Replication Protein A (hsRPA) is required for multiple cellular processes in DNA metabolism including DNA repair, replication and recombination. It binds single-stranded DNA with high affinity and interacts specifically with multiple proteins. hsRPA forms a heterotrimeric complex composed of 70-, 32- and 14-kDa subunits (henceforth RPA70, RPA32, and RPA14). The N-terminal 168 residues of RPA70 form a structurally distinct domain that stimulates DNA polymerase alpha activity, interacts with several transcriptional activators including tumor suppressor p53, and during the cell cycle it signals escape from the DNA damage induced G2/M checkpoint. We have solved the global fold of the fragment corresponding to this domain (RPA70 delta 169) and we find residues 8-108 of the N-terminal domain are structured. The remaining C-terminal residues are unstructured and may form a flexible linker to the DNA-binding domain of RPA70. The globular region forms a five-stranded anti-parallel beta-barrel. The ends of the barrel are capped by short helices. Two loops on one side of the barrel form a large basic cleft which is a likely site for binding the acidic motifs of transcriptional activators. Many lethal or conditional lethal yeast point mutants map to this cleft, whereas no mutations with severe phenotype have been found in the linker region. | ||
==About this Structure== | ==About this Structure== | ||
1EWI 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:// | 1EWI 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=1EWI OCA]. | ||
==Reference== | ==Reference== | ||
| Line 14: | Line 13: | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Daughdrill, G | [[Category: Daughdrill, G W.]] | ||
[[Category: Gomes, X.]] | [[Category: Gomes, X.]] | ||
[[Category: Isern, N | [[Category: Isern, N G.]] | ||
[[Category: Jacobs, D | [[Category: Jacobs, D M.]] | ||
[[Category: Lipton, A | [[Category: Lipton, A S.]] | ||
[[Category: Lowry, D | [[Category: Lowry, D F.]] | ||
[[Category: Wold, M | [[Category: Wold, M S.]] | ||
[[Category: 5-stranded anti-parallel]] | [[Category: 5-stranded anti-parallel]] | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:32:13 2008'' | ||
Revision as of 13:32, 21 February 2008
|
HUMAN REPLICATION PROTEIN A: GLOBAL FOLD OF THE N-TERMINAL RPA-70 DOMAIN REVEALS A BASIC CLEFT AND FLEXIBLE C-TERMINAL LINKER
OverviewOverview
Human Replication Protein A (hsRPA) is required for multiple cellular processes in DNA metabolism including DNA repair, replication and recombination. It binds single-stranded DNA with high affinity and interacts specifically with multiple proteins. hsRPA forms a heterotrimeric complex composed of 70-, 32- and 14-kDa subunits (henceforth RPA70, RPA32, and RPA14). The N-terminal 168 residues of RPA70 form a structurally distinct domain that stimulates DNA polymerase alpha activity, interacts with several transcriptional activators including tumor suppressor p53, and during the cell cycle it signals escape from the DNA damage induced G2/M checkpoint. We have solved the global fold of the fragment corresponding to this domain (RPA70 delta 169) and we find residues 8-108 of the N-terminal domain are structured. The remaining C-terminal residues are unstructured and may form a flexible linker to the DNA-binding domain of RPA70. The globular region forms a five-stranded anti-parallel beta-barrel. The ends of the barrel are capped by short helices. Two loops on one side of the barrel form a large basic cleft which is a likely site for binding the acidic motifs of transcriptional activators. Many lethal or conditional lethal yeast point mutants map to this cleft, whereas no mutations with severe phenotype have been found in the linker region.
About this StructureAbout this Structure
1EWI is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Human replication protein A: global fold of the N-terminal RPA-70 domain reveals a basic cleft and flexible C-terminal linker., Jacobs DM, Lipton AS, Isern NG, Daughdrill GW, Lowry DF, Gomes X, Wold MS, J Biomol NMR. 1999 Aug;14(4):321-31. PMID:10526407
Page seeded by OCA on Thu Feb 21 12:32:13 2008