1npe
From Proteopedia
(New page: 200px<br /><applet load="1npe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1npe, resolution 2.3Å" /> '''Crystal structure of ...) |
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| - | [[Image:1npe.jpg|left|200px]]<br /><applet load="1npe" size=" | + | [[Image:1npe.jpg|left|200px]]<br /><applet load="1npe" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1npe, resolution 2.3Å" /> | caption="1npe, resolution 2.3Å" /> | ||
'''Crystal structure of Nidogen/Laminin Complex'''<br /> | '''Crystal structure of Nidogen/Laminin Complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Basement membranes are fundamental to tissue organization and physiology | + | Basement membranes are fundamental to tissue organization and physiology in all metazoans. The interaction between laminin and nidogen is crucial to the assembly of basement membranes. The structure of the interacting domains reveals a six-bladed Tyr-Trp-Thr-Asp (YWTD) beta-propeller domain in nidogen bound to laminin epidermal-growth-factor-like (LE) modules III3-5 in laminin (LE3-5). Laminin LE module 4 binds to an amphitheatre-shaped surface on the pseudo-6-fold axis of the beta-propeller, and LE module 3 binds over its rim. A Phe residue that shutters the water-filled central aperture of the beta-propeller, the rigidity of the amphitheatre, and high shape complementarity enable the construction of an evolutionarily conserved binding surface for LE4 of unprecedentedly high affinity for its small size. Hypermorphic mutations in the Wnt co-receptor LRP5 (refs 6-9) suggest that a similar YWTD beta-propeller interface is used to bind ligands that function in developmental pathways. A related interface, but shifted off-centre from the pseudo-6-fold axis and lacking the shutter over the central aperture, is used in the low-density lipoprotein receptor for an intramolecular interaction that is regulated by pH in receptor recycling. |
==About this Structure== | ==About this Structure== | ||
| - | 1NPE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with CD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1NPE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=CD:'>CD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NPE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Liu, J | + | [[Category: Liu, J H.]] |
| - | [[Category: Springer, T | + | [[Category: Springer, T A.]] |
[[Category: Takagi, J.]] | [[Category: Takagi, J.]] | ||
| - | [[Category: Wang, J | + | [[Category: Wang, J H.]] |
| - | [[Category: Yang, Y | + | [[Category: Yang, Y T.]] |
[[Category: CD]] | [[Category: CD]] | ||
[[Category: basement membrane]] | [[Category: basement membrane]] | ||
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[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:08:35 2008'' |
Revision as of 12:08, 21 February 2008
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Crystal structure of Nidogen/Laminin Complex
Overview
Basement membranes are fundamental to tissue organization and physiology in all metazoans. The interaction between laminin and nidogen is crucial to the assembly of basement membranes. The structure of the interacting domains reveals a six-bladed Tyr-Trp-Thr-Asp (YWTD) beta-propeller domain in nidogen bound to laminin epidermal-growth-factor-like (LE) modules III3-5 in laminin (LE3-5). Laminin LE module 4 binds to an amphitheatre-shaped surface on the pseudo-6-fold axis of the beta-propeller, and LE module 3 binds over its rim. A Phe residue that shutters the water-filled central aperture of the beta-propeller, the rigidity of the amphitheatre, and high shape complementarity enable the construction of an evolutionarily conserved binding surface for LE4 of unprecedentedly high affinity for its small size. Hypermorphic mutations in the Wnt co-receptor LRP5 (refs 6-9) suggest that a similar YWTD beta-propeller interface is used to bind ligands that function in developmental pathways. A related interface, but shifted off-centre from the pseudo-6-fold axis and lacking the shutter over the central aperture, is used in the low-density lipoprotein receptor for an intramolecular interaction that is regulated by pH in receptor recycling.
About this Structure
1NPE is a Protein complex structure of sequences from Mus musculus with as ligand. Full crystallographic information is available from OCA.
Reference
Complex between nidogen and laminin fragments reveals a paradigmatic beta-propeller interface., Takagi J, Yang Y, Liu JH, Wang JH, Springer TA, Nature. 2003 Aug 21;424(6951):969-74. PMID:12931195
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