Structural highlights
Function
[TRFL_BUBBU] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The three-dimensional structure of diferric buffalo lactoferrin has been determined at 3.3 A resolution. The structure was solved by molecular replacement using the coordinates of diferric human lactoferrin as a search model and was refined by simulated annealing (X-PLOR). The final model comprises 5316 protein atoms for all 689 residues, two Fe(3+) and two CO(3)(2-) ions. The final R factor was 21.8% for 11 711 reflections in the resolution range 17.0-3.3 A. The folding of buffalo lactoferrin is essentially similar to that of the other members of the transferrin family. The significant differences are found in the dimensions of the binding cleft and the interlobe orientation. The interlobe interactions are predominantly hydrophobic in nature, thus facilitating the sliding of two lobes owing to external forces. The interdomain interactions are comparable in the N and C lobes.
Structure of buffalo lactoferrin at 3.3 A resolution at 277 K.,Karthikeyan S, Yadav S, Paramasivam M, Srinivasan A, Singh TP Acta Crystallogr D Biol Crystallogr. 2000 Jun;56(Pt 6):684-9. PMID:10818344[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Karthikeyan S, Yadav S, Paramasivam M, Srinivasan A, Singh TP. Structure of buffalo lactoferrin at 3.3 A resolution at 277 K. Acta Crystallogr D Biol Crystallogr. 2000 Jun;56(Pt 6):684-9. PMID:10818344
