<p>A/ HAMP3 wt and mutant peptides. In the last panel I365S (light grey) and I365S M427T (dark grey) isoforms are shown in an overlay. B/ HAMP4 wt and mutant peptides. The orientation of the peptides is from up (N-terminus) to down (C-terminus) or from right to left (A). Solely, the side chains from amino-acids of the connector proximal helices are displayed. Residues potentially involved in interactions are labelled; modified residues are written in italics. In overlaid models, the wild-type peptide is shaded in light grey, the mutant peptide in dark grey.</p
HAMP domains are small, dimeric, four-helical bundles found exclusively in a class of signalling pro...
<p><b>A:</b> Schematic depiction and <b>B:</b> predicted 3D structural models of wild-type ApoC1 (H1...
<p>(a) Multiple conformations of the peptides bound to an SH3 domain were collected from various cry...
<p>A/ HAMP1 wild-type (wt) and mutant peptides. B/ HAMP2 wt and mutant peptides. The orientation of ...
<p>The amino-acid sequences of the six HAMP domains of the Bos1 protein were aligned with Clustal W....
<p>(A) Schematics of canonical HAMP connected to input and output domain; (B) Side view of the struc...
<p>(A) Crystal structure of Aer2 1–172 proteins, with HAMP1 colored blue (WT), purple (L44H), and gr...
Homodimeric receptors with one or two transmembrane (TM) segments per monomer are universal to life ...
HAMP domain is a ubiquitous module of bacterial and archaeal two-component signaling systems. Consid...
HAMP domains convert an extracellular sensory input into an intracellular signaling response in a wi...
<p>Conformation of the F124 pair is closely related to the conformation of the whole HAMP domain. Th...
<p>The peptide chains are shown as blue and gray ribbons, and the tRNA molecules are shown as atomic...
<div><p>(A) Overall structure of the HAUSP TRAF-like domain bound to MDM2 peptide is shown in a ribb...
<p>Structural models of the hA3G N-terminal domain. The models were constructed by homology modeling...
<p>The predicted low-energy model of the Aha1-N domain bound to the Hsp90 dimer is shown in (A) in a...
HAMP domains are small, dimeric, four-helical bundles found exclusively in a class of signalling pro...
<p><b>A:</b> Schematic depiction and <b>B:</b> predicted 3D structural models of wild-type ApoC1 (H1...
<p>(a) Multiple conformations of the peptides bound to an SH3 domain were collected from various cry...
<p>A/ HAMP1 wild-type (wt) and mutant peptides. B/ HAMP2 wt and mutant peptides. The orientation of ...
<p>The amino-acid sequences of the six HAMP domains of the Bos1 protein were aligned with Clustal W....
<p>(A) Schematics of canonical HAMP connected to input and output domain; (B) Side view of the struc...
<p>(A) Crystal structure of Aer2 1–172 proteins, with HAMP1 colored blue (WT), purple (L44H), and gr...
Homodimeric receptors with one or two transmembrane (TM) segments per monomer are universal to life ...
HAMP domain is a ubiquitous module of bacterial and archaeal two-component signaling systems. Consid...
HAMP domains convert an extracellular sensory input into an intracellular signaling response in a wi...
<p>Conformation of the F124 pair is closely related to the conformation of the whole HAMP domain. Th...
<p>The peptide chains are shown as blue and gray ribbons, and the tRNA molecules are shown as atomic...
<div><p>(A) Overall structure of the HAUSP TRAF-like domain bound to MDM2 peptide is shown in a ribb...
<p>Structural models of the hA3G N-terminal domain. The models were constructed by homology modeling...
<p>The predicted low-energy model of the Aha1-N domain bound to the Hsp90 dimer is shown in (A) in a...
HAMP domains are small, dimeric, four-helical bundles found exclusively in a class of signalling pro...
<p><b>A:</b> Schematic depiction and <b>B:</b> predicted 3D structural models of wild-type ApoC1 (H1...
<p>(a) Multiple conformations of the peptides bound to an SH3 domain were collected from various cry...