<p>(A) Interhelical interactions of coiled coil within the asymmetric unit of the seleno-methionine crystal are shown. The residues in the positions a and d of heptad repeats are presented as a stick model at the top panel. Close-up views of three different parts are shown. The amino acid residues that participated in the interhelical interactions are labelled. L; Left, M; Middle, R; Right. (B) Helical wheel presentation of the heptad repeats in SYCP1 CC. Interhelical charged interactions are indicated by a red-line connecting paired residues. Charged residues and hydrophobic residues are colored blue and red, respectively.</p
<p>Structural representations of A) Utr-SR1, B) Utr-SR1-L and C) Dys-SR1 showing the burial of hydro...
The bZIP transcription factors make up a family of long α-helical proteins that dimerize based on a ...
<p>Details of the asymmetric dimer interface are shown in the left expanded view. The interfacial el...
<p>(<b>A</b>) Ribbon (left) and surface (right) diagram of the crystal structure of <i>c</i>HAD dime...
The synaptonemal complex protein 1 (SYCP1) is the main structural element of transverse filaments (T...
<p>A. The dimeric structure of CARMA1 CARD and close-up view of the interacting residues in the inte...
<div><p>(A) Helical-wheel representation shows an end-on view of the structure. Opposing <b>a</b> an...
<p>(a) The symmetric intersubunit interface, found only between subunits A (in green) and C (in oran...
<p>The subunits of the homo-dimer are shown in blue and orange respectively. The secondary structure...
<p>Subunit A and B are colored green and red, respectively. Amino acid residues in the dimeric inter...
The short coiled coil protein (SCOC) forms a complex with fasciculation and elongation protein zeta ...
The short coiled coil protein (SCOC) forms a complex with fasciculation and elongation protein zeta ...
<p>A) The canonical dimer (blue and green) found in the asymmetric unit. Two dimerization helices (α...
The short coiled coil protein (SCOC) forms a complex with fasciculation and elongation protein zeta ...
The environment of amino acid residues in protein tertiary structures and three types of interfaces ...
<p>Structural representations of A) Utr-SR1, B) Utr-SR1-L and C) Dys-SR1 showing the burial of hydro...
The bZIP transcription factors make up a family of long α-helical proteins that dimerize based on a ...
<p>Details of the asymmetric dimer interface are shown in the left expanded view. The interfacial el...
<p>(<b>A</b>) Ribbon (left) and surface (right) diagram of the crystal structure of <i>c</i>HAD dime...
The synaptonemal complex protein 1 (SYCP1) is the main structural element of transverse filaments (T...
<p>A. The dimeric structure of CARMA1 CARD and close-up view of the interacting residues in the inte...
<div><p>(A) Helical-wheel representation shows an end-on view of the structure. Opposing <b>a</b> an...
<p>(a) The symmetric intersubunit interface, found only between subunits A (in green) and C (in oran...
<p>The subunits of the homo-dimer are shown in blue and orange respectively. The secondary structure...
<p>Subunit A and B are colored green and red, respectively. Amino acid residues in the dimeric inter...
The short coiled coil protein (SCOC) forms a complex with fasciculation and elongation protein zeta ...
The short coiled coil protein (SCOC) forms a complex with fasciculation and elongation protein zeta ...
<p>A) The canonical dimer (blue and green) found in the asymmetric unit. Two dimerization helices (α...
The short coiled coil protein (SCOC) forms a complex with fasciculation and elongation protein zeta ...
The environment of amino acid residues in protein tertiary structures and three types of interfaces ...
<p>Structural representations of A) Utr-SR1, B) Utr-SR1-L and C) Dys-SR1 showing the burial of hydro...
The bZIP transcription factors make up a family of long α-helical proteins that dimerize based on a ...
<p>Details of the asymmetric dimer interface are shown in the left expanded view. The interfacial el...