1hlh: Difference between revisions

Line 1:

~~{{Theoretical_model}}~~

==PROPOSED STRUCTURE FOR THE DNA-BINDING DOMAIN OF THE HELIX- LOOP-HELIX FAMILY OF EUKARYOTIC GENE REGULATORY PROTEINS==

== Structural highlights ==

<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HLH FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hlh FirstGlance], [http://www.ebi.ac.uk/pdbsum/1hlh PDBsum]</span></td></tr>

<table>

== Publication Abstract from PubMed ==

A modelled tertiary structure for the dimeric HLH domain of the E47 protein is presented. Structural information was obtained from the aligned sequences of > 40 members of the HLH family. The information was used to model each monomer as an alpha-helical hairpin, with knobs-into-holes packing of side-chains as found in antiparallel coiled-coil. The dimer forms a four-helix bundle with additional knobs-into-holes packing at the dimer interface. The size and electrostatic properties of core-forming residues are all accounted for in the model. The model does not violate any known properties of protein structure. The monomers are related by two-fold rotational symmetry, in agreement with the observed DNA-binding sites which are imperfect inverted repeats. The N-terminal basic region, in which DNA binding and base specificity reside, forms the first part of helix 1. A prediction based on the model structure is that the HLH domains do not bind to DNA in its B form but require a partially unwound conformation in order to enter the major groove.

~~[[Image~~:~~1hlh~~.~~png|left|200px]]~~

Proposed structure for the DNA-binding domain of the helix-loop-helix family of eukaryotic gene regulatory proteins.,Gibson TJ, Thompson JD, Abagyan RA Protein Eng. 1993 Jan;6(1):41-50. PMID:8433970<ref>PMID:8433970</ref>

~~{{STRUCTURE_1hlh| PDB=1hlh | SCENE= }}~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~===PROPOSED STRUCTURE FOR THE DNA-BINDING DOMAIN OF THE HELIX- LOOP-HELIX FAMILY OF EUKARYOTIC GENE REGULATORY PROTEINS===~~

== References ==

~~{{ABSTRACT_PUBMED_8433970}}~~

__TOC__

</StructureSection>

==~~Reference~~==

<~~ref group="xtra">PMID:008433970<~~/~~ref~~><~~references group="xtra"~~/>

[[Category: Abagyan, R A]]

[[Category: Gibson, T J]]

[[Category: Thompson, J D]]

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-{{Theoretical_model}}
+==PROPOSED STRUCTURE FOR THE DNA-BINDING DOMAIN OF THE HELIX- LOOP-HELIX FAMILY OF EUKARYOTIC GENE REGULATORY PROTEINS==
+<StructureSection load='1hlh' size='340' side='right' caption='[[1hlh]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HLH FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hlh FirstGlance], [http://www.ebi.ac.uk/pdbsum/1hlh PDBsum]</span></td></tr>
+<table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A modelled tertiary structure for the dimeric HLH domain of the E47 protein is presented. Structural information was obtained from the aligned sequences of &gt; 40 members of the HLH family. The information was used to model each monomer as an alpha-helical hairpin, with knobs-into-holes packing of side-chains as found in antiparallel coiled-coil. The dimer forms a four-helix bundle with additional knobs-into-holes packing at the dimer interface. The size and electrostatic properties of core-forming residues are all accounted for in the model. The model does not violate any known properties of protein structure. The monomers are related by two-fold rotational symmetry, in agreement with the observed DNA-binding sites which are imperfect inverted repeats. The N-terminal basic region, in which DNA binding and base specificity reside, forms the first part of helix 1. A prediction based on the model structure is that the HLH domains do not bind to DNA in its B form but require a partially unwound conformation in order to enter the major groove.
-[[Image:1hlh.png|left|200px]]
+Proposed structure for the DNA-binding domain of the helix-loop-helix family of eukaryotic gene regulatory proteins.,Gibson TJ, Thompson JD, Abagyan RA Protein Eng. 1993 Jan;6(1):41-50. PMID:8433970<ref>PMID:8433970</ref>
-{{STRUCTURE_1hlh|  PDB=1hlh  |  SCENE=  }}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-===PROPOSED STRUCTURE FOR THE DNA-BINDING DOMAIN OF THE HELIX- LOOP-HELIX FAMILY OF EUKARYOTIC GENE REGULATORY PROTEINS===
+== References ==
+<references/>
-{{ABSTRACT_PUBMED_8433970}}
+__TOC__
+</StructureSection>
-==Reference==
-<ref group="xtra">PMID:008433970</ref><references group="xtra"/>
 [[Category: Abagyan, R A]]
 [[Category: Gibson, T J]]
 [[Category: Thompson, J D]]