The functions of proteins are largely determined by their three-dimensional (3D) structures. Loop modeling tries to predict the conformation of a relatively short stretch of protein backbone and sidechain. It is a difficult problem due to conformational variability. Recently, AlphaFold2 has achieved outstanding results in 3-D protein structure prediction and is expected to perform well on loop modeling. In this paper, we investigate the performances of AlphaFold2 variants on popular loop modeling benchmark datasets and propose an efficient protocol of using AlphaFold2 for loop modeling, called IAFLoop. To predict the structure of a loop region, IAFLoop gives a moderately extended segment of the target loop region as input to AlphaFold2, runs a fast version of AlphaFold2 using a reduced database without ensembling, and uses RMSD based consensus scores to select the final output models. Our experimental results on benchmark datasets show that IAFLoop generated highly accurate loop models. It achieves comparable performance to the original application of AlphaFold2 in terms of RMSD error, and achieving much better results on some targets, while only using half of the time. Compared to the best previous methods, IAFLoop reduces the RMSD error by almost half on the 8-residual loop dataset, and more than 70% on the 12-residual loop dataset.