Hox protein: Difference between revisions

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[[Image:Hox-intro.jpg|thumb|left|250px|Figure 1: Crystal structure of Exd-Scr-DNA ternary complex; [http://proteopedia.com/wiki/index.php/2r5z PDB ID# 2R5Z]<ref name="joshi">Joshi R, Passner JM, Rohs R, Jain R, Sosinsky A, Crickmore MA, Jacob V, Aggarwal AK, Honig B, Mann RS. Functional specificity of a Hox protein mediated by the recognition of minor groove structure. Cell. 2007;131(3):530-43. [http://www.ncbi.nlm.nih.gov/pubmed/17981120 PMID:17981120]</ref>. The Hox protein Scr (yellow) and its cofactor Exd (blue) bind to its specific ''fkh20'' site.]]  
[[Image:Hox-intro.jpg|thumb|left|250px|Figure 1: Crystal structure of Exd-Scr-DNA ternary complex; [http://proteopedia.com/wiki/index.php/2r5z PDB ID# 2R5Z]<ref name="joshi">Joshi R, Passner JM, Rohs R, Jain R, Sosinsky A, Crickmore MA, Jacob V, Aggarwal AK, Honig B, Mann RS. Functional specificity of a Hox protein mediated by the recognition of minor groove structure. Cell. 2007;131(3):530-43. [http://www.ncbi.nlm.nih.gov/pubmed/17981120 PMID:17981120]</ref>. The Hox protein Scr (yellow) and its cofactor Exd (blue) bind to its specific ''fkh20'' site.]]  


[[Image:Cell.jpg|thumb|right|300px|Figure 2: Hox proteins require a cofactor to achieve high binding specificity in order to execute their distinct functions in developing various parts of the fly embryo <ref name="slattery">Slattery M, Riley T, Liu P, Abe N, Gomez-Alcala P, Dror I, Zhou T, Rohs R, Honig B, Bussemaker HJ, Mann RS. Cofactor binding evokes latent differences in DNA binding specificity between Hox proteins. Cell. 2011;147(6):1270-82. [http://www.ncbi.nlm.nih.gov/pubmed/22153072 PMID:22153072]</ref>. Elsevier/Cell Press has provided permission for usage of this figure.]]
[[Image:Cell.jpg|thumb|right|300px|Figure 2: Hox proteins require a cofactor to achieve high binding specificity in order to execute their distinct functions in developing various parts of the fly embryo. Elsevier/Cell Press has provided permission for usage of this figure<ref name="slattery">Slattery M, Riley T, Liu P, Abe N, Gomez-Alcala P, Dror I, Zhou T, Rohs R, Honig B, Bussemaker HJ, Mann RS. Cofactor binding evokes latent differences in DNA binding specificity between Hox proteins. Cell. 2011;147(6):1270-82. [http://www.ncbi.nlm.nih.gov/pubmed/22153072 PMID:22153072]</ref>.]]


Hox proteins are transcription factors that play a key role in the '''embryonic development''' across species by activating and repressing genes. In ''Drosophila,'' eight Hox proteins are responsible for the development of different body segments of the fly, such as its antennae, wings, or legs. Hox proteins execute their distinct functions through binding to similar but different in vivo binding sites<ref>Mann RS, Lelli KM, Joshi R. Hox specificity unique roles for cofactors and collaborators. Curr Top Dev Biol. 2009;88:63-101. [http://www.ncbi.nlm.nih.gov/pubmed/19651302 PMID:19651302]</ref>. This page discusses molecular mechanisms through which Hox proteins recognize their DNA targets with very high binding specificity. <br/>
Hox proteins are transcription factors that play a key role in the '''embryonic development''' across species by activating and repressing genes. In ''Drosophila,'' eight Hox proteins are responsible for the development of different body segments of the fly, such as its antennae, wings, or legs. Hox proteins execute their distinct functions through binding to similar but different in vivo binding sites<ref>Mann RS, Lelli KM, Joshi R. Hox specificity unique roles for cofactors and collaborators. Curr Top Dev Biol. 2009;88:63-101. [http://www.ncbi.nlm.nih.gov/pubmed/19651302 PMID:19651302]</ref>. This page discusses molecular mechanisms through which Hox proteins recognize their DNA targets with very high binding specificity. <br/>
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=Acknowledgements=
=Acknowledgements=
This Proteopedia page originates from the partnership of the Rohs Laboratory at the University of Southern California with La Cañada High School. This partnership was initiated by Remo Rohs and Patty Compeau in September 2011 as '''Bioinformatics Institute''', which is part of the Institutes of the 21st Century. Furthermore, technical help by Proteopedia editors Eran Hodis, Eric Martz, Jaime Prilusky, and Joel Sussman is acknowledged.<br/>
This Proteopedia page originates from the partnership of the Rohs Laboratory at the University of Southern California with La Cañada High School. This partnership was initiated by Remo Rohs and Patty Compeau in September 2011 as '''Bioinformatics Institute''', which is part of the Institutes of the 21st Century. Advice and technical help by Proteopedia editors Eran Hodis, Eric Martz, Jaime Prilusky, and Joel Sussman is acknowledged.<br/>


=References=
=References=
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