1msr

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

MODEL OF THE DIMERIC TRANSMEMBRANE DOMAIN OF GLYCOPHORIN A

spinqualitylabelsall models 1msr Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum, ProSAT Publication Abstract from PubMed A more global search method, using fewer assumptions, has been used to predict the structure of the dimeric transmembrane region of the protein glycophorin A. The resulting model significantly differs from that previously determined. In particular, the arrangement between the two transmembrane helices is now more symmetric resulting in improved interaction energies and an increased buried surface area. An increase in the van der Waals interaction energy due to tighter packing compensates for the loss of the interhelical hydrogen bond observed between Thr-87 of each helix in the previous model. Improved prediction for the structure of the dimeric transmembrane domain of glycophorin A obtained through global searching.,Adams PD, Engelman DM, Brunger AT Proteins. 1996 Nov;26(3):257-61. PMID:8953647 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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