<p>FHA domains contain five conserved residues, Gly (a) and (b), His (c), Arg (d), Ser (e) and Asn (f). Each conserved residue is shown in red letters. Blue and pink represent loops and peptides, respectively. The sidechain atoms are shown in bond representation. Red, blue and green dash lines indicate H-bond, salt-bridge and van der Waals interactions, respectively. This structure is taken from a molecular dynamics (MD) snapshot of the Rad53-FHA1 complex.</p
<p>Sequences forming a secondary structure, α helix and β sheet, are in bold italic and italic forma...
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Amino acid residues, which play important roles in protein function, are often conserved. Here, we a...
<p>We summarize the key domain–peptide interactions of Rad53-FHA1 (a), Dun1-FHA (b) and Ki67-FHA (c)...
<p>The trajectories from MD simulations show the flexibility of Rad53-FHA1 (A), Dun1-FHA (B) and Ki6...
<p>The three FHA domains, Rad53-FHA1, Dun1-FHA and Ki67-FHA, are shown in (a), (b) and (c), respecti...
<p>The fold of the FHA domain includes 11 β sheets linked by loops. The loops that connect different...
<p>(a) Sequence alignment of the FHA domain from different proteins. The β strands and loops are in ...
[[sponsorship]]基因體研究中心,生物化學研究所[[note]]已出版;[SCI];有審查制度;不具代表性[[note]]http://gateway.isiknowledge.com/g...
SummaryFHA domains are well established as phospho-dependent binding modules mediating signal transd...
<p>(A) Model of FHA. The dotted vertical lines at the right side of the protein model indicate the a...
<p>PDB ID's and corresponding protein identities are as follows, 4h87: the kanadaptin-FHA domain, 3v...
<p><b>A</b>: Rab5a (PDB entry 1R2Q) secondary structure and amino acid residues colored from variabl...
Key interactions with H34/R34, D38/E38, and Y83/H83 are shown in the blue square (A), the orange squ...
<p>(A) Combined contact plots for the head domain and part of the rod domain showing the probability...
<p>Sequences forming a secondary structure, α helix and β sheet, are in bold italic and italic forma...
[[sponsorship]]基因體研究中心,生物化學研究所[[note]]已出版;[SCI];有審查制度;不具代表性[[note]]http://gateway.isiknowledge.com/g...
Amino acid residues, which play important roles in protein function, are often conserved. Here, we a...
<p>We summarize the key domain–peptide interactions of Rad53-FHA1 (a), Dun1-FHA (b) and Ki67-FHA (c)...
<p>The trajectories from MD simulations show the flexibility of Rad53-FHA1 (A), Dun1-FHA (B) and Ki6...
<p>The three FHA domains, Rad53-FHA1, Dun1-FHA and Ki67-FHA, are shown in (a), (b) and (c), respecti...
<p>The fold of the FHA domain includes 11 β sheets linked by loops. The loops that connect different...
<p>(a) Sequence alignment of the FHA domain from different proteins. The β strands and loops are in ...
[[sponsorship]]基因體研究中心,生物化學研究所[[note]]已出版;[SCI];有審查制度;不具代表性[[note]]http://gateway.isiknowledge.com/g...
SummaryFHA domains are well established as phospho-dependent binding modules mediating signal transd...
<p>(A) Model of FHA. The dotted vertical lines at the right side of the protein model indicate the a...
<p>PDB ID's and corresponding protein identities are as follows, 4h87: the kanadaptin-FHA domain, 3v...
<p><b>A</b>: Rab5a (PDB entry 1R2Q) secondary structure and amino acid residues colored from variabl...
Key interactions with H34/R34, D38/E38, and Y83/H83 are shown in the blue square (A), the orange squ...
<p>(A) Combined contact plots for the head domain and part of the rod domain showing the probability...
<p>Sequences forming a secondary structure, α helix and β sheet, are in bold italic and italic forma...
[[sponsorship]]基因體研究中心,生物化學研究所[[note]]已出版;[SCI];有審查制度;不具代表性[[note]]http://gateway.isiknowledge.com/g...
Amino acid residues, which play important roles in protein function, are often conserved. Here, we a...