1ck4
From Proteopedia
(New page: 200px<br /><applet load="1ck4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ck4, resolution 2.20Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1ck4.gif|left|200px]]<br /><applet load="1ck4" size=" | + | [[Image:1ck4.gif|left|200px]]<br /><applet load="1ck4" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ck4, resolution 2.20Å" /> | caption="1ck4, resolution 2.20Å" /> | ||
'''CRYSTAL STRUCTURE OF RAT A1B1 INTEGRIN I-DOMAIN.'''<br /> | '''CRYSTAL STRUCTURE OF RAT A1B1 INTEGRIN I-DOMAIN.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The alpha1beta1 integrin is a major cell surface receptor for collagen. | + | 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 Structure== | ==About this Structure== | ||
| - | 1CK4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 1CK4 is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Gotwals, P | + | [[Category: Gotwals, P J.]] |
[[Category: Karpusas, M.]] | [[Category: Karpusas, M.]] | ||
[[Category: Koteliansky, V.]] | [[Category: Koteliansky, V.]] | ||
[[Category: Nolte, M.]] | [[Category: Nolte, M.]] | ||
| - | [[Category: Pepinsky, R | + | [[Category: Pepinsky, R B.]] |
| - | [[Category: Venyaminov, S | + | [[Category: Venyaminov, S Y.]] |
[[Category: adhesion]] | [[Category: adhesion]] | ||
[[Category: collagen]] | [[Category: collagen]] | ||
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[[Category: metal binding]] | [[Category: metal binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:52 2008'' |
Revision as of 10:06, 21 February 2008
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CRYSTAL STRUCTURE OF RAT A1B1 INTEGRIN I-DOMAIN.
Overview
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 Structure
1CK4 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
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:10386626
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