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TitleA Disulfide-Free Single-Domain V(L) Intrabody with Blocking Activity towards Huntingtin Reveals a Novel Mode of Epitope Recognition.
Journal, issue, pagesJ. Mol. Biol., Vol. 414, Page 337-355, Year 2011
Publish dateFeb 11, 2010 (structure data deposition date)
AuthorsSchiefner, A. / Chatwell, L. / Korner, J. / Neumaier, I. / Colby, D.W. / Volkmer, R. / Wittrup, K.D. / Skerra, A.
External linksJ. Mol. Biol. / PubMed:21968397
MethodsX-ray diffraction
Resolution2.05 - 2.6 Å
Structure data

PDB-3lrg:
Structure of anti-huntingtin VL domain
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

PDB-3lrh:
Structure of anti-huntingtin VL domain in complex with huntingtin peptide
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-IMD:
IMIDAZOLE

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM / Huntington's disease / Huntingtin / Variable light chain domain / Intrabody / Immunoglobulin

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