1ck4: Difference between revisions
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[[Image:1ck4.gif|left|200px]] | [[Image:1ck4.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF RAT A1B1 INTEGRIN I-DOMAIN.''' | {{Structure | ||
|PDB= 1ck4 |SIZE=350|CAPTION= <scene name='initialview01'>1ck4</scene>, resolution 2.20Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
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'''CRYSTAL STRUCTURE OF RAT A1B1 INTEGRIN I-DOMAIN.''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1CK4 is a [ | 1CK4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CK4 OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of the alpha1beta1 integrin I-domain: insights into integrin I-domain function., Nolte M, Pepinsky RB, Venyaminov SYu, Koteliansky V, Gotwals PJ, Karpusas M, FEBS Lett. 1999 Jun 11;452(3):379-85. PMID:[http:// | Crystal structure of the alpha1beta1 integrin I-domain: insights into integrin I-domain function., Nolte M, Pepinsky RB, Venyaminov SYu, Koteliansky V, Gotwals PJ, Karpusas M, FEBS Lett. 1999 Jun 11;452(3):379-85. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10386626 10386626] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: metal binding]] | [[Category: metal binding]] | ||
''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 10:25:23 2008'' | ||
Revision as of 11:25, 20 March 2008
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CRYSTAL STRUCTURE OF RAT A1B1 INTEGRIN I-DOMAIN.
OverviewOverview
The alpha1beta1 integrin is a major cell surface receptor for collagen. Ligand binding is mediated, in part, through a 200 amino acid inserted 'I'-domain contained in the extracellular part of the integrin alpha chain. Integrin I-domains contain a divalent cation binding (MIDAS) site and require cations to interact with integrin ligands. We have determined the crystal structure of recombinant I-domain from the rat alpha1beta1 integrin at 2.2 A resolution in the absence of divalent cations. The alpha1 I-domain adopts the dinucleotide binding fold that is characteristic of all I-domain structures that have been solved to date and has a structure very similar to that of the closely related alpha2beta1 I-domain which also mediates collagen binding. A unique feature of the alpha1 I-domain crystal structure is that the MIDAS site is occupied by an arginine side chain from another I-domain molecule in the crystal, in place of a metal ion. This interaction supports a proposed model for ligand-induced displacement of metal ions. Circular dichroism spectra determined in the presence of Ca2+, Mg2+ and Mn2+ indicate that no changes in the structure of the I-domain occur upon metal ion binding in solution. Metal ion binding induces small changes in UV absorption spectra, indicating a change in the polarity of the MIDAS site environment.
About this StructureAbout this Structure
1CK4 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the alpha1beta1 integrin I-domain: insights into integrin I-domain function., Nolte M, Pepinsky RB, Venyaminov SYu, Koteliansky V, Gotwals PJ, Karpusas M, FEBS Lett. 1999 Jun 11;452(3):379-85. PMID:10386626
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