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| - | [[Image:1j4o.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1j4o| PDB=1j4o | SCENE= }} | | {{STRUCTURE_1j4o| PDB=1j4o | SCENE= }} |
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| - | '''REFINED NMR STRUCTURE OF THE FHA1 DOMAIN OF YEAST RAD53'''
| + | ===REFINED NMR STRUCTURE OF THE FHA1 DOMAIN OF YEAST RAD53=== |
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| - | ==Overview==
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| - | Rad53, a yeast checkpoint protein involved in regulating the repair of DNA damage, contains two forkhead-associated domains, FHA1 and FHA2. Previous combinatorial library screening has shown that FHA1 strongly selects peptides containing a pTXXD motif. Subsequent location of this motif within the sequence of Rad9, the target protein, coupled with spectroscopic analysis has led to identification of a tight binding sequence that is likely the binding site of FHA1: (188)SLEV(pT)EADATFVQ(200). We present solution structures of FHA1 in complex with this pT-peptide and with another Rad9-derived pT-peptide that has ca 30-fold lower affinity, (148)KKMTFQ(pT)PTDPLE(160). Both complexes showed intermolecular NOEs predominantly between three peptide residues (pT, +1, and +2 residues) and five FHA1 residues (S82, R83, S85, T106, and N107). Furthermore, the following interactions were implicated on the basis of chemical shift perturbations and structural analysis: the phosphate group of the pT residue with the side-chain amide group of N86 and the guanidino group of R70, and the carboxylate group of Asp (at the +3 position) with the guanidino group of R83. The generated structures revealed a similar binding mode adopted by these two peptides, suggesting that pT and the +3 residue Asp are the major contributors to binding affinity and specificity, while +1 and +2 residues could provide additional fine-tuning. It was also shown that FHA1 does not bind to the corresponding pS-peptides or a related pY-peptide. We suggest that differentiation between pT and pS-peptides by FHA1 can be attributed to hydrophobic interactions between the methyl group of the pT residue and the aliphatic protons of R83, S85, and T106 from FHA1.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11846567}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11846567 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11846567}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1J4O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J4O OCA]. | + | 1J4O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J4O OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Rad53]] | | [[Category: Rad53]] |
| | [[Category: Rad9]] | | [[Category: Rad9]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:47:59 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:29:41 2008'' |
Revision as of 11:29, 1 July 2008
Template:STRUCTURE 1j4o
REFINED NMR STRUCTURE OF THE FHA1 DOMAIN OF YEAST RAD53
Template:ABSTRACT PUBMED 11846567
About this Structure
1J4O is a Single protein structure of sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA.
Reference
Solution structures of two FHA1-phosphothreonine peptide complexes provide insight into the structural basis of the ligand specificity of FHA1 from yeast Rad53., Yuan C, Yongkiettrakul S, Byeon IJ, Zhou S, Tsai MD, J Mol Biol. 2001 Nov 30;314(3):563-75. PMID:11846567
Page seeded by OCA on Tue Jul 1 14:29:41 2008
