User:Yash Patankar/Sandbox 1: Difference between revisions
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Each Hsp90 monomer consists of an N-teminal domain, a middle (M) domain and a C-terminal domain. The N-terminal domain (a.a. 1-216) is formed by a twisted six stranded β-sheet on one face of the monomer and six α-helices, leading to a two-layer sandwich. The charged linker connecting the N-terminal and M domains consists of poorly conserved and low complexity repeats of amino acids and thus is an obstacle to obtaining crystals showing strong diffraction patterns and was thus omitted from the structure determination process and replaced by an eight residue-loop. The middle domain is subdivided into a large (a.a. 273-409) and small (a.a. 435-525) domain, both of which are α-β-α domains. The C-terminal domain (a.a. 525-709) consists of a three stranded β-sheet a five α-helices. A three-helix coil forms the constitutive dimerization interface for the protomer as shown in figure ______. The residues 678-709 provide the binding sequence for TPR-domain co-chaperones, but they are not crystallized as they are highly disordered (Ali et al., 2006). | Each Hsp90 monomer consists of an N-teminal domain, a middle (M) domain and a C-terminal domain. The N-terminal domain (a.a. 1-216) is formed by a twisted six stranded β-sheet on one face of the monomer and six α-helices, leading to a two-layer sandwich. The charged linker connecting the N-terminal and M domains consists of poorly conserved and low complexity repeats of amino acids and thus is an obstacle to obtaining crystals showing strong diffraction patterns and was thus omitted from the structure determination process and replaced by an eight residue-loop. The middle domain is subdivided into a large (a.a. 273-409) and small (a.a. 435-525) domain, both of which are α-β-α domains. The C-terminal domain (a.a. 525-709) consists of a three stranded β-sheet a five α-helices. A three-helix coil forms the constitutive dimerization interface for the protomer as shown in figure ______. The residues 678-709 provide the binding sequence for TPR-domain co-chaperones, but they are not crystallized as they are highly disordered (Ali et al., 2006). | ||
Sba1/p23 molecules bind to Hsp90 in the junction of the N-terminal domains of the dimer. | Sba1/p23 molecules bind to Hsp90 in the junction of the N-terminal domains of the dimer. Figure shows bound Sba1/p23 and Hsp90. | ||
==Conformation of Hsp90== | ==Conformation of Hsp90== | ||
