Auxin binding protein

Auxin binding protein
crystal structure of auxin-binding protein 1 in complex with 1-naphthalene acetic acid
Identifiers
Symbol Auxin_BP
Pfam PF02041
Pfam clan CL0029
InterPro IPR000526
SCOP 1lr5

In molecular biology, the auxin binding protein family is a family of proteins which bind auxin.[1] They are located in the lumen of the endoplasmic reticulum (ER). The primary structure of these proteins contains an N-terminal hydrophobic leader sequence of 30-40 amino acids, which could represent a signal for translocation of the protein to the ER.[2][3] The mature protein comprises around 165 residues, and contains a number of potential N-glycosylation sites. In vitro transport studies have demonstrated co-translational glycosylation.[3] Retention within the lumen of the ER correlates with an additional signal located at the C terminus, represented by the sequence Lys-Asp-Glu-Leu, known to be responsible for preventing secretion of proteins from the lumen of the ER in eukaryotic cells.[2][3]

References

  1. ^ Woo EJ, Marshall J, Bauly J, Chen JG, Venis M, Napier RM et al. (2002). "Crystal structure of auxin-binding protein 1 in complex with auxin.". EMBO J 21 (12): 2877–85. doi:10.1093/emboj/cdf291. PMC 126050. PMID 12065401. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=126050. 
  2. ^ a b Hesse T, Feldwisch J, Balshusemann D, Bauw G, Puype M, Vandekerckhove J, Lobler M, Klambt D, Schell J, Palme K (September 1989). "Molecular cloning and structural analysis of a gene from Zea mays (L.) coding for a putative receptor for the plant hormone auxin". EMBO J. 8 (9): 2453–61. PMC 401229. PMID 2555179. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=401229. 
  3. ^ a b c Palme K, Hesse T, Campos N, Garbers C, Yanofsky MF, Schell J (February 1992). "Molecular analysis of an auxin binding protein gene located on chromosome 4 of Arabidopsis". Plant Cell 4 (2): 193–201. doi:10.1105/tpc.4.2.193. PMC 160120. PMID 1321684. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=160120. 

This article incorporates text from the public domain Pfam and InterPro IPR000526