Intrinsically Disordered Protein: Difference between revisions
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Many [[X-ray crystallography|crystallographic]] structures have missing loops -- that is, ranges of amino acids with no [[atomic coordinate file|atomic coordinates]] in the model. These "gaps" in the model are often thought to be artifacts of inadvertant disorder in the crystal. In some cases, these gaps may be alerting us to the presence of intrinsically disordered loops in an otherwise folded protein. Such gaps are the basis for the [[#Protein disorder predictors|DISOPRED2 disorder prediction server]]. [[FirstGlance in Jmol]] offers [[Temperature_value#Missing_Residues|one method for locating and visualizaing such gaps]]. | Many [[X-ray crystallography|crystallographic]] structures have missing loops -- that is, ranges of amino acids with no [[atomic coordinate file|atomic coordinates]] in the model. These "gaps" in the model are often thought to be artifacts of inadvertant disorder in the crystal. In some cases, these gaps may be alerting us to the presence of intrinsically disordered loops in an otherwise folded protein. Such gaps are the basis for the [[#Protein disorder predictors|DISOPRED2 disorder prediction server]]. [[FirstGlance in Jmol]] offers [[Temperature_value#Missing_Residues|one method for locating and visualizaing such gaps]]. | ||
Despite the existence of compelling evidence for IUPs and intrinsically disordered loops beginning in 1990, many current textbooks of biochemistry and even some monographs on protein structure fail to mention intrinsic disorder and its importance for protein function<ref>PMID: 18831774</ref><ref>Martz, E. Book review of <i>Introduction to protein science—architecture, function, and genomics: Lesk, Arthur M.</i>. <i>Biochem. Mol. Biol. Educ.</i> 33:144-5 (2006). [http://dx.doi.org/10.1002/bmb.2005.494033022442 DOI: 10.1002/bmb.2005.494033022442]</ref>. In 2011, Chouard provided a readable and informative overview of IUPs and how some of them function<ref>PMID: 21390105</ref>. | Despite the existence of compelling evidence for IUPs and intrinsically disordered loops beginning in 1990<ref name="struhl1990" /><ref>PMID: 2236048</ref>, many current textbooks of biochemistry and even some monographs on protein structure fail to mention intrinsic disorder and its importance for protein function<ref>PMID: 18831774</ref><ref>Martz, E. Book review of <i>Introduction to protein science—architecture, function, and genomics: Lesk, Arthur M.</i>. <i>Biochem. Mol. Biol. Educ.</i> 33:144-5 (2006). [http://dx.doi.org/10.1002/bmb.2005.494033022442 DOI: 10.1002/bmb.2005.494033022442]</ref>. In 2011, Chouard provided a readable and informative overview of IUPs and how some of them function<ref>PMID: 21390105</ref>. | ||
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* Membrane fusion and membrane transport, e.g. isolated components of the SNARE complex<ref>PMID: 10048921</ref> | * Membrane fusion and membrane transport, e.g. isolated components of the SNARE complex<ref>PMID: 10048921</ref> | ||
* DNA recognition molecules, e.g. the basic DNA-binding region of the leucine zipper protein, GCN4<ref>PMID: 2145515</ref> | * DNA recognition molecules, e.g. the basic DNA-binding region of the leucine zipper protein, GCN4<ref name="struhl1990">PMID: 2145515</ref> | ||
* Protein-RNA recognition, e.g. ribosomal proteins, such as L11-C76<ref>PMID: 8989327</ref> and [[Large Ribosomal Subunit of Haloarcula#The proteins:|several others]]<ref>PMID:10937989</ref> | * Protein-RNA recognition, e.g. ribosomal proteins, such as L11-C76<ref>PMID: 8989327</ref> and [[Large Ribosomal Subunit of Haloarcula#The proteins:|several others]]<ref>PMID:10937989</ref> | ||
