1ewi
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(New page: 200px<br /> <applet load="1ewi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ewi" /> '''HUMAN REPLICATION PROTEIN A: GLOBAL FOLD OF...)
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Revision as of 14:40, 12 November 2007
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HUMAN REPLICATION PROTEIN A: GLOBAL FOLD OF THE N-TERMINAL RPA-70 DOMAIN REVEALS A BASIC CLEFT AND FLEXIBLE C-TERMINAL LINKER
Overview
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
1EWI is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
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