2i1p | pdb_00002i1p

Solution structure of the twelfth cysteine-rich ligand-binding repeat in rat megalin

spinqualitylabelsall models 2i1p, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2i1p is a 1 chain structure with sequence from Buffalo rat. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [LRP2_RAT] Acts together with cubilin to mediate HDL endocytosis (By similarity). Receptor-mediated uptake of polybasic drugs such as aprotinin, aminoglycosides and polymyxin B. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Megalin, an approx. 600 kDa transmembrane glycoprotein that acts as multi-ligand transporter, is a member of the low density lipoprotein receptor gene family. Several cysteine-rich repeats, each consisting of about 40 residues, are responsible for the multispecific binding of ligands. The solution structure of the twelfth cysteine-rich ligand-binding repeat with class A motif found in megalin features two short beta-strands and two helical turns, yielding the typical fold with a I-III, II-V and IV-VI disulfide bridge connectivity pattern and a calcium coordination site at the C-terminal end. The resulting differences in electrostatic surface potential compared to other ligand-binding modules of this gene family, however, may be responsible for the functional divergence. Solution structure of the twelfth cysteine-rich ligand-binding repeat in rat megalin.,Wolf CA, Dancea F, Shi M, Bade-Noskova V, Ruterjans H, Kerjaschki D, Lucke C J Biomol NMR. 2007 Apr;37(4):321-8. Epub 2007 Jan 24. PMID:17245526 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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