1l3y: Difference between revisions
New page: left|200px<br /> <applet load="1l3y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l3y" /> '''INTEGRIN EGF-LIKE MODULE 3 FROM THE BETA-2 ... |
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'''INTEGRIN EGF-LIKE MODULE 3 FROM THE BETA-2 SUBUNIT'''<br /> | '''INTEGRIN EGF-LIKE MODULE 3 FROM THE BETA-2 SUBUNIT'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1L3Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 1L3Y is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: integrin]] | [[Category: integrin]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:16:31 2008'' | ||
Revision as of 17:16, 15 February 2008
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INTEGRIN EGF-LIKE MODULE 3 FROM THE BETA-2 SUBUNIT
OverviewOverview
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.
DiseaseDisease
Known disease associated with this structure: Leukocyte adhesion deficiency OMIM:[600065]
About this StructureAbout this Structure
1L3Y is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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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