3ldn | pdb_00003ldn

Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in apo form

spinqualitylabelsall models 3ldn, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ldn is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3ldl, 3ldo, 3ldp, 3ldq Gene: HSPA5, GRP78 (Homo sapiens) Resources: FirstGlance, OCA, RCSB, PDBsum Disease [GRP78_HUMAN] Note=Autoantigen in rheumatoid arthritis. Function [GRP78_HUMAN] Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Publication Abstract from PubMed 78 kDa glucose-regulated protein (Grp78) is a heat shock protein (HSP) involved in protein folding that plays a role in cancer cell proliferation. Binding of adenosine-derived inhibitors to Grp78 was characterized by surface plasmon resonance and isothermal titration calorimetry. The most potent compounds were 13 (VER-155008) with K(D) = 80 nM and 14 with K(D) = 60 nM. X-ray crystal structures of Grp78 bound to ATP, ADPnP, and adenosine derivative 10 revealed differences in the binding site between Grp78 and homologous proteins. Adenosine-Derived Inhibitors of 78 kDa Glucose Regulated Protein (Grp78) ATPase: Insights into Isoform Selectivity.,Macias AT, Williamson DS, Allen N, Borgognoni J, Clay A, Daniels Z, Dokurno P, Drysdale MJ, Francis GL, Graham CJ, Howes R, Matassova N, Murray JB, Parsons R, Shaw T, Surgenor AE, Terry L, Wang Y, Wood M, Massey AJ J Med Chem. 2011 May 20. PMID:21526763 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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