2i1p
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(New page: 200px<br /><applet load="2i1p" size="450" color="white" frame="true" align="right" spinBox="true" caption="2i1p" /> '''Solution structure of the twelfth cysteine-r...)
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Revision as of 09:58, 21 November 2007
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Solution structure of the twelfth cysteine-rich ligand-binding repeat in rat megalin
Overview
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.
About this Structure
2I1P is a Single protein structure of sequence from Rattus norvegicus with CA as ligand. Full crystallographic information is available from OCA.
Reference
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
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