bHLH-PAS Proteins: Their Structure and Intrinsic Disorder
The basic helix-loop-helix/Per-ARNT-SIM (bHLH-PAS) proteins are a class of transcriptional regulators, commonly occurring in living organisms and highly conserved among vertebrates and invertebrates. These proteins exhibit a relatively well-conserved domain structure: the bHLH domain located at the...
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description | The basic helix-loop-helix/Per-ARNT-SIM (bHLH-PAS) proteins are a class of transcriptional regulators, commonly occurring in living organisms and highly conserved among vertebrates and invertebrates. These proteins exhibit a relatively well-conserved domain structure: the bHLH domain located at the N-terminus, followed by PAS-A and PAS-B domains. In contrast, their C-terminal fragments present significant variability in their primary structure and are unique for individual proteins. C-termini were shown to be responsible for the specific modulation of protein action. In this review, we present the current state of knowledge, based on NMR and X-ray analysis, concerning the structural properties of bHLH-PAS proteins. It is worth noting that all determined structures comprise only selected domains (bHLH and/or PAS). At the same time, substantial parts of proteins, comprising their long C-termini, have not been structurally characterized to date. Interestingly, these regions appear to be intrinsically disordered (IDRs) and are still a challenge to research. We aim to emphasize the significance of IDRs for the flexibility and function of bHLH-PAS proteins. Finally, we propose modern NMR methods for the structural characterization of the IDRs of bHLH-PAS proteins. |
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These proteins exhibit a relatively well-conserved domain structure: the bHLH domain located at the N-terminus, followed by PAS-A and PAS-B domains. In contrast, their C-terminal fragments present significant variability in their primary structure and are unique for individual proteins. C-termini were shown to be responsible for the specific modulation of protein action. In this review, we present the current state of knowledge, based on NMR and X-ray analysis, concerning the structural properties of bHLH-PAS proteins. It is worth noting that all determined structures comprise only selected domains (bHLH and/or PAS). At the same time, substantial parts of proteins, comprising their long C-termini, have not been structurally characterized to date. Interestingly, these regions appear to be intrinsically disordered (IDRs) and are still a challenge to research. We aim to emphasize the significance of IDRs for the flexibility and function of bHLH-PAS proteins. Finally, we propose modern NMR methods for the structural characterization of the IDRs of bHLH-PAS proteins.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms20153653</identifier><identifier>PMID: 31357385</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Amino acid sequence ; Amino acids ; Animals ; Basic Helix-Loop-Helix Transcription Factors - chemistry ; Basic Helix-Loop-Helix Transcription Factors - metabolism ; Cancer ; Computational Biology - methods ; Dimerization ; Domains ; Genes ; Humans ; Hypoxia ; Immune system ; Intrinsically Disordered Proteins - chemistry ; Intrinsically Disordered Proteins - metabolism ; Invertebrates ; Ligands ; Mammals ; Metabolism ; Models, Anatomic ; Organs ; Physiology ; Protein Binding ; Protein Conformation ; Protein Interaction Domains and Motifs ; Protein Multimerization ; Protein-Serine-Threonine Kinases - chemistry ; Protein-Serine-Threonine Kinases - metabolism ; Proteins ; Review ; Structure-Activity Relationship ; Transcription factors ; Tumorigenesis ; Tumors</subject><ispartof>International journal of molecular sciences, 2019-07, Vol.20 (15), p.3653</ispartof><rights>2019. This work is licensed under https://creativecommons.org/licenses/by/4.0/ (the “License”). 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Finally, we propose modern NMR methods for the structural characterization of the IDRs of bHLH-PAS proteins.</description><subject>Amino acid sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Basic Helix-Loop-Helix Transcription Factors - chemistry</subject><subject>Basic Helix-Loop-Helix Transcription Factors - metabolism</subject><subject>Cancer</subject><subject>Computational Biology - methods</subject><subject>Dimerization</subject><subject>Domains</subject><subject>Genes</subject><subject>Humans</subject><subject>Hypoxia</subject><subject>Immune system</subject><subject>Intrinsically Disordered Proteins - chemistry</subject><subject>Intrinsically Disordered Proteins - metabolism</subject><subject>Invertebrates</subject><subject>Ligands</subject><subject>Mammals</subject><subject>Metabolism</subject><subject>Models, Anatomic</subject><subject>Organs</subject><subject>Physiology</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Protein Interaction Domains and Motifs</subject><subject>Protein Multimerization</subject><subject>Protein-Serine-Threonine Kinases - chemistry</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Proteins</subject><subject>Review</subject><subject>Structure-Activity Relationship</subject><subject>Transcription factors</subject><subject>Tumorigenesis</subject><subject>Tumors</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpdkc1LAzEQxYMotlZvnmXBiwdXk8wm2fUglPrRQsFC6zlks1mbsh812RX8793SWqqnGXg_3szjIXRJ8B1Agu_tqvQUEwacwRHqk4jSEGMujg_2HjrzfoUxBcqSU9QDAkxAzPooScfTcTgbzoOZqxtjK_8QLJbGumDeuFY3rTOBqrJgUjWuE60OnqyvXWbcOTrJVeHNxW4O0PvL82I0Dqdvr5PRcBrqiNAmVEwwk-Q60ymLVAwkJjSmeWqoIDpLKIkEEGxykykSxboLQjllTGjAJEuBwwA9bn3XbVqaTJvuE1XItbOlct-yVlb-VSq7lB_1l-Q8YZyQzuBmZ-Dqz9b4RpbWa1MUqjJ16yWlXODuthAdev0PXdWtq7p4kgIAjwTDG8PbLaVd7b0z-f4ZguWmE3nYSYdfHQbYw78lwA8HpIX-</recordid><startdate>20190726</startdate><enddate>20190726</enddate><creator>Kolonko, Marta</creator><creator>Greb-Markiewicz, Beata</creator><general>MDPI AG</general><general>MDPI</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-2831-439X</orcidid><orcidid>https://orcid.org/0000-0003-4153-3391</orcidid></search><sort><creationdate>20190726</creationdate><title>bHLH-PAS Proteins: Their Structure and Intrinsic Disorder</title><author>Kolonko, Marta ; Greb-Markiewicz, Beata</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c412t-a575e9fcdcb54a83181282fbe271cd92147310efeda148c015262557c301db363</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Amino acid sequence</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Basic Helix-Loop-Helix Transcription Factors - chemistry</topic><topic>Basic Helix-Loop-Helix Transcription Factors - metabolism</topic><topic>Cancer</topic><topic>Computational Biology - methods</topic><topic>Dimerization</topic><topic>Domains</topic><topic>Genes</topic><topic>Humans</topic><topic>Hypoxia</topic><topic>Immune system</topic><topic>Intrinsically Disordered Proteins - chemistry</topic><topic>Intrinsically Disordered Proteins - metabolism</topic><topic>Invertebrates</topic><topic>Ligands</topic><topic>Mammals</topic><topic>Metabolism</topic><topic>Models, Anatomic</topic><topic>Organs</topic><topic>Physiology</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Protein Interaction Domains and Motifs</topic><topic>Protein Multimerization</topic><topic>Protein-Serine-Threonine Kinases - chemistry</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Proteins</topic><topic>Review</topic><topic>Structure-Activity Relationship</topic><topic>Transcription factors</topic><topic>Tumorigenesis</topic><topic>Tumors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kolonko, Marta</creatorcontrib><creatorcontrib>Greb-Markiewicz, Beata</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Research Library (Corporate)</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>International journal of molecular sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kolonko, Marta</au><au>Greb-Markiewicz, Beata</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>bHLH-PAS Proteins: Their Structure and Intrinsic Disorder</atitle><jtitle>International journal of molecular sciences</jtitle><addtitle>Int J Mol Sci</addtitle><date>2019-07-26</date><risdate>2019</risdate><volume>20</volume><issue>15</issue><spage>3653</spage><pages>3653-</pages><issn>1422-0067</issn><issn>1661-6596</issn><eissn>1422-0067</eissn><abstract>The basic helix-loop-helix/Per-ARNT-SIM (bHLH-PAS) proteins are a class of transcriptional regulators, commonly occurring in living organisms and highly conserved among vertebrates and invertebrates. These proteins exhibit a relatively well-conserved domain structure: the bHLH domain located at the N-terminus, followed by PAS-A and PAS-B domains. In contrast, their C-terminal fragments present significant variability in their primary structure and are unique for individual proteins. C-termini were shown to be responsible for the specific modulation of protein action. In this review, we present the current state of knowledge, based on NMR and X-ray analysis, concerning the structural properties of bHLH-PAS proteins. It is worth noting that all determined structures comprise only selected domains (bHLH and/or PAS). At the same time, substantial parts of proteins, comprising their long C-termini, have not been structurally characterized to date. Interestingly, these regions appear to be intrinsically disordered (IDRs) and are still a challenge to research. We aim to emphasize the significance of IDRs for the flexibility and function of bHLH-PAS proteins. Finally, we propose modern NMR methods for the structural characterization of the IDRs of bHLH-PAS proteins.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>31357385</pmid><doi>10.3390/ijms20153653</doi><orcidid>https://orcid.org/0000-0002-2831-439X</orcidid><orcidid>https://orcid.org/0000-0003-4153-3391</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Amino acid sequence Amino acids Animals Basic Helix-Loop-Helix Transcription Factors - chemistry Basic Helix-Loop-Helix Transcription Factors - metabolism Cancer Computational Biology - methods Dimerization Domains Genes Humans Hypoxia Immune system Intrinsically Disordered Proteins - chemistry Intrinsically Disordered Proteins - metabolism Invertebrates Ligands Mammals Metabolism Models, Anatomic Organs Physiology Protein Binding Protein Conformation Protein Interaction Domains and Motifs Protein Multimerization Protein-Serine-Threonine Kinases - chemistry Protein-Serine-Threonine Kinases - metabolism Proteins Review Structure-Activity Relationship Transcription factors Tumorigenesis Tumors |
title | bHLH-PAS Proteins: Their Structure and Intrinsic Disorder |
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