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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[[Image:2i1p.jpg|left|200px]]<br /><applet load="2i1p" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="2i1p" />
'''Solution structure of the twelfth cysteine-rich ligand-binding repeat in rat megalin'''<br />
'''Solution structure of the twelfth cysteine-rich ligand-binding repeat in rat megalin'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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2I1P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2I1P OCA].
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2I1P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I1P OCA].
==Reference==
==Reference==
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[[Category: Rueterjans, H.]]
[[Category: Rueterjans, H.]]
[[Category: Shi, M.]]
[[Category: Shi, M.]]
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[[Category: Wolf, C.A.]]
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[[Category: Wolf, C A.]]
[[Category: CA]]
[[Category: CA]]
[[Category: calcium cage]]
[[Category: calcium cage]]
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[[Category: low density lipoprotein receptor]]
[[Category: low density lipoprotein receptor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:06:09 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:48:07 2008''

Revision as of 15:48, 21 February 2008


2i1p

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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 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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