Region 1 |
Type: | Disordered |
Name: | N-terminal acidic (A-) domain |
Location: | 1 - 455 |
Length: | 455 |
Region sequence: |
MGDGTEFVVRSDREDKKLAEDRISDEQVVKNELVRSDEVRDDNEDEVFEEAIGSENDEQE EEEDPKRELFESDDLPLVETLKSSMVEHEVEDFEEAVGDLDETSSNEGGVKDFTAVGESH GAGEAEFDVLATKMNGDKGEGGGGGSYDKVESSLDVVDTTENATSTNTNGSNLAAEHVGI ENGKTHSFLGNGIASPKNKEVVAEVIPKDDGIEEPWNDGIEVDNWEERVDGIQTEQEVEE GEGTTENQFEKRTEEEVVEGEGTSKNLFEKQTEQDVVEGEGTSKDLFENGSVCMDSESEA ERNGETGAAYTSNIVTNASGDNEVSSAVTSSPLEESSSGEKGETEGDSTCLKPEQHLASS PHSYPESTEVHSNSGSPGVTSREHKPVQSANGGHDVQSPQPNKELEKQQSSRVHVDPEIT ENSHVETEPEVVSSVSPTESRSNPAALPPARPAGL |
Modification type: | Native
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PDB: | |
Structural/functional type: | Function arises via a disorder to order transition |
Functional classes: | Molecular recognition effectors
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Functional subclasses: | Substrate/ligand binding
Protein-protein binding
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Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (298 K; pH: 8; )
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References:
- Richardson LG, Jelokhani-Niaraki M, Smith MD. "The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains." BMC Biochem. 2009; 10(1): 35. PubMed: 20042108
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Comments:The A-domain was shown experimentally to be disordered under non-denaturing conditions, and underwent structural changes characteristic of IDPs at extremes of temperature and pH. Furthermore, in the presence of 50% TFE, the A-domain gained considerable structure.
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