1l3y
From Proteopedia
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| - | [[Image:1l3y.jpg|left|200px]] | + | [[Image:1l3y.jpg|left|200px]] |
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| - | '''INTEGRIN EGF-LIKE MODULE 3 FROM THE BETA-2 SUBUNIT''' | + | {{Structure |
| + | |PDB= 1l3y |SIZE=350|CAPTION= <scene name='initialview01'>1l3y</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''INTEGRIN EGF-LIKE MODULE 3 FROM THE BETA-2 SUBUNIT''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1L3Y is a [ | + | 1L3Y is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L3Y OCA]. |
==Reference== | ==Reference== | ||
| - | Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation., Beglova N, Blacklow SC, Takagi J, Springer TA, Nat Struct Biol. 2002 Apr;9(4):282-7. PMID:[http:// | + | Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation., Beglova N, Blacklow SC, Takagi J, Springer TA, Nat Struct Biol. 2002 Apr;9(4):282-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11896403 11896403] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: integrin]] | [[Category: integrin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:26:02 2008'' |
Revision as of 10:26, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
INTEGRIN EGF-LIKE MODULE 3 FROM THE BETA-2 SUBUNIT
Contents |
Overview
Cysteine-rich repeats in the integrin beta subunit stalk region relay activation signals to the ligand-binding headpiece. The NMR solution structure and disulfide bond connectivity of Cys-rich module-3 of the integrin beta2 subunit reveal a nosecone-shaped variant of the EGF fold, termed an integrin-EGF (I-EGF) domain. Interdomain contacts between I-EGF domains 2 and 3 observed by NMR support a model in which the modules are related by an approximate two-fold screw axis in an extended arrangement. Our findings complement a 3.1 A crystal structure of the extracellular portion of integrin alphaVbeta3, which lacks an atomic model for I-EGF2 and a portion of I-EGF3. The disulfide connectivity of I-EGF3 chemically assigned here differs from the pairings suggested in the alphaVbeta3 structure. Epitopes that become exposed upon integrin activation and residues that restrain activation are defined in beta2 I-EGF domains 2 and 3. Superposition on the alphaVbeta3 structure reveals that they are buried. This observation suggests that the highly bent alphaVbeta3 structure represents the inactive conformation and that release of contacts with I-EGF modules 2 and 3 triggers a switchblade-like opening motion extending the integrin into its active conformation.
Disease
Known disease associated with this structure: Leukocyte adhesion deficiency OMIM:[600065]
About this Structure
1L3Y is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation., Beglova N, Blacklow SC, Takagi J, Springer TA, Nat Struct Biol. 2002 Apr;9(4):282-7. PMID:11896403
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