User talk:Anders Lewisesquerre: Difference between revisions
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== Structure == | == Structure == | ||
<scene name='10/1078788/Bdnf/1'>BDNF</scene><Structure load='1b8m' size='350' frame='true' align='right' caption='BDNF' scene='10/1078788/Bdnf/1' /> is a 13kDa protein that belongs to the nerve growth factor (NGF) family. In a broader sense, BDNF is part of the cystine-knot cytokine superfamily. A cystine-knot is a structural motif characterized by three intertwined disulfide bonds that form a knot. This <scene name='10/1078788/Bdnf_disulfide_bonds_2/1'>Cystine knot</scene>, which has three disulfide bonds and is likely a key structural feature that allows binding to the TrkB receptor. | <scene name='10/1078788/Bdnf/1'>BDNF</scene><Structure load='1b8m' size='350' frame='true' align='right' caption='BDNF' scene='10/1078788/Bdnf/1' /> is a 13kDa protein that belongs to the nerve growth factor (NGF) family. In a broader sense, BDNF is part of the cystine-knot cytokine superfamily. A cystine-knot is a structural motif characterized by three intertwined disulfide bonds that form a knot. This <scene name='10/1078788/Bdnf_disulfide_bonds_2/1'>Cystine knot</scene>, which has three disulfide bonds and is likely a key structural feature that allows binding to the TrkB receptor. The protein is composed mostly of 𝛽-sheets, with the exception of the small, single alpha helical turn from amino acid residues 22-26. There are also notable flexible regions in the protein that consist of 𝛽-turns, and intrinsically disordered regions (IDRs). A ConSurf-DB analysis was done on BDNF to identify conserved sequences on the protein. The analysis results identified residues running along the long middle portions of 𝛽-sheets. This may provide insight into regions of BDNF receptor binding, where the less conserved regions may vary from species to species due to the differing physiology of such species. | ||
