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1hlh
From Proteopedia
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| - | + | ==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 > 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | == | + | == References == |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | < | + | |
[[Category: Abagyan, R A]] | [[Category: Abagyan, R A]] | ||
[[Category: Gibson, T J]] | [[Category: Gibson, T J]] | ||
[[Category: Thompson, J D]] | [[Category: Thompson, J D]] | ||
Revision as of 12:42, 28 September 2014
PROPOSED STRUCTURE FOR THE DNA-BINDING DOMAIN OF THE HELIX- LOOP-HELIX FAMILY OF EUKARYOTIC GENE REGULATORY PROTEINS
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