1ck4: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ck4]] is a 2 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CK4 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1ck4]] is a 2 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CK4 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ck4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ck4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ck4 RCSB], [http://www.ebi.ac.uk/pdbsum/1ck4 PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ck4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ck4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ck4 RCSB], [http://www.ebi.ac.uk/pdbsum/1ck4 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Gotwals, P J | [[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 B | [[Category: Pepinsky, R B]] | ||
[[Category: Venyaminov, S Y | [[Category: Venyaminov, S Y]] | ||
[[Category: Adhesion]] | [[Category: Adhesion]] | ||
[[Category: Collagen]] | [[Category: Collagen]] | ||
Revision as of 02:56, 23 December 2014
CRYSTAL STRUCTURE OF RAT A1B1 INTEGRIN I-DOMAIN.CRYSTAL STRUCTURE OF RAT A1B1 INTEGRIN I-DOMAIN.
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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