Conformational flexibility in SUMO-1 protein (PDB:1a5r). The central part shows relatively ordered structure. Conversely, the N- and C-terminal regions (left and right, respectively) show ‘intrinsic disorder’, although a short helical region persists in the N-terminal tail. Ten alternative NMR models were morphed. Secondary structure elements: α-helices (red), β-strands (blue arrows). [1]
In molecular biology, an intrinsically disordered protein (IDP) is a protein that lacks a fixed or ordered three-dimensional structure,[2][3][4] typically in the absence of its macromolecular interaction partners, such as other proteins or RNA. IDPs range from fully unstructured to partially structured and include random coil, molten globule-like aggregates, or flexible linkers in large multi-domain proteins. They are sometimes considered as a separate class of proteins along with globular, fibrous and membrane proteins.[5]
IDPs are a very large and functionally important class of proteins and their discovery has disproved the idea that three-dimensional structures of proteins must be fixed to accomplish their biological functions. For example, IDPs have been identified to participate in weak multivalent interactions that are highly cooperative and dynamic, lending them importance in DNA regulation and in cell signaling.[6][7] Many IDPs can also adopt a fixed three-dimensional structure after binding to other macromolecules. Overall, IDPs are different from structured proteins in many ways and tend to have distinctive function, structure, sequence, interactions, evolution and regulation.[8]
^Majorek K, Kozlowski L, Jakalski M, Bujnicki JM (December 18, 2008). "First Steps of Protein Structure Prediction" (PDF). In Bujnicki J (ed.). Prediction of Protein Structures, Functions, and Interactions. John Wiley & Sons, Ltd. pp. 39–62. doi:10.1002/9780470741894.ch2. ISBN 9780470517673.
^Dunker AK, Lawson JD, Brown CJ, Williams RM, Romero P, Oh JS, Oldfield CJ, Campen AM, Ratliff CM, Hipps KW, Ausio J, Nissen MS, Reeves R, Kang C, Kissinger CR, Bailey RW, Griswold MD, Chiu W, Garner EC, Obradovic Z (2001). "Intrinsically disordered protein". Journal of Molecular Graphics & Modelling. 19 (1): 26–59. CiteSeerX 10.1.1.113.556. doi:10.1016/s1093-3263(00)00138-8. PMID 11381529.
^Dyson HJ, Wright PE (March 2005). "Intrinsically unstructured proteins and their functions". Nature Reviews Molecular Cell Biology. 6 (3): 197–208. doi:10.1038/nrm1589. PMID 15738986. S2CID 18068406.
^Dunker AK, Silman I, Uversky VN, Sussman JL (December 2008). "Function and structure of inherently disordered proteins". Current Opinion in Structural Biology. 18 (6): 756–64. doi:10.1016/j.sbi.2008.10.002. PMID 18952168.
^Andreeva A, Howorth D, Chothia C, Kulesha E, Murzin AG (January 2014). "SCOP2 prototype: a new approach to protein structure mining". Nucleic Acids Research. 42 (Database issue): D310–4. doi:10.1093/nar/gkt1242. PMC 3964979. PMID 24293656.
^Mir M, Stadler MR, Ortiz SA, Hannon CE, Harrison MM, Darzacq X, Eisen MB (December 2018). Singer RH, Struhl K, Crocker J (eds.). "Dynamic multifactor hubs interact transiently with sites of active transcription in Drosophila embryos". eLife. 7: e40497. doi:10.7554/eLife.40497. PMC 6307861. PMID 30589412.
^van der Lee R, Buljan M, Lang B, Weatheritt RJ, Daughdrill GW, Dunker AK, et al. (July 2014). "Classification of intrinsically disordered regions and proteins". Chemical Reviews. 114 (13): 6589–6631. doi:10.1021/cr400525m. PMC 4095912. PMID 24773235.
and 27 Related for: Intrinsically disordered proteins information
PMID 21501695. Oldfield CJ, Dunker AK (2014). "Intrinsicallydisorderedproteins and intrinsicallydisorderedprotein regions". Annual Review of Biochemistry...
a different fold separated by intrinsicallydisordered regions. These are referred to as multi-domain proteins. Proteins may also be classified based on...
function of the flexible protein, extending the structure-function paradigm from folded proteins to intrinsicallydisorderedproteins. The calculation of ensembles...
the less stable variants are intrinsicallydisorderedproteins. These proteins exist and function in a relatively 'disordered' state lacking a stable tertiary...
disorder, and phase separation behavior of these repetitive polypeptides make them an interesting class of minimal synthetic intrinsicallydisordered...
Tardigrade specific proteins are types of intrinsicallydisorderedproteins specific to tardigrades. These proteins help tardigrades survive desiccation...
has its strengths and weaknesses but they all struggle with intrinsicallydisorderedproteins without any clearly defined tertiary structure as the essence...
including freezing and desiccation. Research has shown that intrinsicallydisorderedproteins in these organisms may work to stabilize cell function and...
biological database of intrinsicallydisorderedproteins (IDPs) and regions (IDRs). DisProt annotations cover state information on the protein but also, when...
"Differential dehydration effects on globular proteins and intrinsicallydisorderedproteins during film formation". Protein Science. 26 (4). Wiley: 718–726. doi:10...
classified as intrinsicallydisorderedproteins. Predicting and analysing proteindisorder is, therefore, an important part of protein structure characterisation...
(un)folded proteins. Biotin 'painting' shows a bias towards predicted Intrinsicallydisorderedproteins. Computational studies of protein folding includes...
theoretical, computational, and experimental approaches to study intrinsicallydisorderedproteins in the context of normal cellular function and neurodegenerative...
switching whether in cancer or in normal cells is that they are Intrinsicallydisorderedproteins (IDPs). That is, they lack a rigid 3D-structure under physiological...
heat-stable proteins essential for microtubule assembly, and since then they have been characterized as intrinsicallydisorderedproteins. Tau proteins are found...
Kurgan L (Jan 2014). "Genome-scale prediction of proteins with long intrinsicallydisordered regions". Proteins. 82 (1): 145–58. doi:10.1002/prot.24348. PMID 23798504...
animals survived such extreme conditions. It was found that intrinsicallydisorderedproteins (IDPs) were highly expressed in response to desiccation in...
unfolded" or intrinsicallydisorderedproteins, characterized by high flexibility and a lack of ordered tertiary structure. These disorderedproteins, referred...
Expansions are less likely, and losses more likely, for intrinsicallydisorderedproteins and for protein domains whose hydrophobic amino acids are further...
oxygen species and xenobiotics, expression of heat shock proteins and intrinsicallydisorderedproteins as well as biosynthesis of polyunsaturated fatty acids...
It is also the name of a protein family, of which MARCKS is the most studied member. They are intrinsicallydisorderedproteins, with an acidic pH, with...
structure-function paradigm the all proteins follow. They are predominately consisted of IntrinsicallyDisorderedProteins (IDP) that are necessary for certain...
plan, a human resources term Internally displaced person Intrinsicallydisorderedproteins International Driving Permit IPD (disambiguation) This disambiguation...
of intrinsicallydisorderedprotein, which continuously change their conformation unless they are bound to a specific partner such as another protein. With...
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