This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1qu0
From Proteopedia
m (Protected "1qu0" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1qu0.png|left|200px]] | ||
| - | |||
{{STRUCTURE_1qu0| PDB=1qu0 | SCENE= }} | {{STRUCTURE_1qu0| PDB=1qu0 | SCENE= }} | ||
| - | |||
===CRYSTAL STRUCTURE OF THE FIFTH LAMININ G-LIKE MODULE OF THE MOUSE LAMININ ALPHA2 CHAIN=== | ===CRYSTAL STRUCTURE OF THE FIFTH LAMININ G-LIKE MODULE OF THE MOUSE LAMININ ALPHA2 CHAIN=== | ||
| + | {{ABSTRACT_PUBMED_10619025}} | ||
| - | + | ==Disease== | |
| + | [[http://www.uniprot.org/uniprot/LAMA2_MOUSE LAMA2_MOUSE]] Note=Defects in Lama2 are a cause of murine muscular dystrophy (dy2J). | ||
| + | |||
| + | ==Function== | ||
| + | [[http://www.uniprot.org/uniprot/LAMA2_MOUSE LAMA2_MOUSE]] Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. | ||
==About this Structure== | ==About this Structure== | ||
| Line 11: | Line 13: | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:010619025</ref><references group="xtra"/> | + | <ref group="xtra">PMID:010619025</ref><references group="xtra"/><references/> |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Hohenester, E.]] | [[Category: Hohenester, E.]] | ||
Revision as of 06:21, 25 March 2013
Contents |
CRYSTAL STRUCTURE OF THE FIFTH LAMININ G-LIKE MODULE OF THE MOUSE LAMININ ALPHA2 CHAIN
Template:ABSTRACT PUBMED 10619025
Disease
[LAMA2_MOUSE] Note=Defects in Lama2 are a cause of murine muscular dystrophy (dy2J).
Function
[LAMA2_MOUSE] Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.
About this Structure
1qu0 is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
- Hohenester E, Tisi D, Talts JF, Timpl R. The crystal structure of a laminin G-like module reveals the molecular basis of alpha-dystroglycan binding to laminins, perlecan, and agrin. Mol Cell. 1999 Nov;4(5):783-92. PMID:10619025
