<p><b>Copyright information:</b></p><p>Taken from "The crystal structure of the putative peptide-binding fragment from the human Hsp40 protein Hdj1"</p><p>http://www.biomedcentral.com/1472-6807/8/3</p><p>BMC Structural Biology 2008;8():3-3.</p><p>Published online 22 Jan 2008</p><p>PMCID:PMC2254625.</p><p></p> Program Pileup from GCG package was utilized to align residues 162–340 of Hdj1 from with similar regions of Hsp40 proteins from (Hsp40-3), (Z66513.1), (Droj-1), (Psi protein) and (Sis1). The amino acid residue numbers of Hdj1 are numbered above the alignment. The residues involved in forming the peptide-binding site of Hdj1 are marked by blue bars. The secondary structures of Hdj1 are shown on top of the alignment. The structural compo...
<p>Residues belonging to the binding site are underlined, residues identified with alanine scanning ...
<p>The TATA-box-like elements are indicated by shading and the dots indicate alignment. Abbreviation...
<p><b>Copyright information:</b></p><p>Taken from "functional characterization of a double histone f...
<p>Human HSP70 (HSPA1A or HSP72), HSPA2, HSPA5 (GRP78 or BiP), HSC70 (HSPA8 or HSP73), HSPA9 (GRP75,...
<p><b>Copyright information:</b></p><p>Taken from "The crystal structure of the putative peptide-bin...
<p><b>Copyright information:</b></p><p>Taken from "The crystal structure of the putative peptide-bin...
Hsp40 is a co-chaperone of Hsp70 that correctly folds polypeptides that exist in non-native forms. T...
<p>The amino acid sequence of ArHsp40-2 from <i>A</i>. <i>franciscana</i> was aligned with type 2 Hs...
<p>Protein sequence alignment of HCMV (strain AD169), EBV (strain B958), and HSV-1 (strain KOS) (Uni...
<p>The amino acid sequences of ArHsp40 and ArHsp40-2 were compared by CLUSTAL OMEGA (<b><a href="htt...
<p>Fully conservative sequences and residues in iron binding sphere are colored grey and dark grey, ...
<p>Multiple sequence alignment of LiSIR2rp1 (Uniprot #Q8I6E4) with ScHst2 (P53686), hSIRT1 (Q96EB6),...
<p>(A) Sequence alignment of C-terminal segment and its neighboring region in HslUs from different o...
<p>The hydrophobic cores of both proteins are marked in red. The charged residues are indicated with...
<p>The crystallographically determined secondary structure elements are depicted below the sequences...
<p>Residues belonging to the binding site are underlined, residues identified with alanine scanning ...
<p>The TATA-box-like elements are indicated by shading and the dots indicate alignment. Abbreviation...
<p><b>Copyright information:</b></p><p>Taken from "functional characterization of a double histone f...
<p>Human HSP70 (HSPA1A or HSP72), HSPA2, HSPA5 (GRP78 or BiP), HSC70 (HSPA8 or HSP73), HSPA9 (GRP75,...
<p><b>Copyright information:</b></p><p>Taken from "The crystal structure of the putative peptide-bin...
<p><b>Copyright information:</b></p><p>Taken from "The crystal structure of the putative peptide-bin...
Hsp40 is a co-chaperone of Hsp70 that correctly folds polypeptides that exist in non-native forms. T...
<p>The amino acid sequence of ArHsp40-2 from <i>A</i>. <i>franciscana</i> was aligned with type 2 Hs...
<p>Protein sequence alignment of HCMV (strain AD169), EBV (strain B958), and HSV-1 (strain KOS) (Uni...
<p>The amino acid sequences of ArHsp40 and ArHsp40-2 were compared by CLUSTAL OMEGA (<b><a href="htt...
<p>Fully conservative sequences and residues in iron binding sphere are colored grey and dark grey, ...
<p>Multiple sequence alignment of LiSIR2rp1 (Uniprot #Q8I6E4) with ScHst2 (P53686), hSIRT1 (Q96EB6),...
<p>(A) Sequence alignment of C-terminal segment and its neighboring region in HslUs from different o...
<p>The hydrophobic cores of both proteins are marked in red. The charged residues are indicated with...
<p>The crystallographically determined secondary structure elements are depicted below the sequences...
<p>Residues belonging to the binding site are underlined, residues identified with alanine scanning ...
<p>The TATA-box-like elements are indicated by shading and the dots indicate alignment. Abbreviation...
<p><b>Copyright information:</b></p><p>Taken from "functional characterization of a double histone f...