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1ck4

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Revision as of 10:43, 19 May 2021

CRYSTAL STRUCTURE OF RAT A1B1 INTEGRIN I-DOMAIN.

Structural highlights

1ck4 is a 2 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ITA1_RAT] Integrin alpha-1/beta-1 is a receptor for laminin and collagen. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen.

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 PubMed

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.

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.

References

↑ Nolte M, Pepinsky RB, Venyaminov SYu, Koteliansky V, Gotwals PJ, Karpusas M. Crystal structure of the alpha1beta1 integrin I-domain: insights into integrin I-domain function. FEBS Lett. 1999 Jun 11;452(3):379-85. PMID:10386626

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ck4"

@@ Line 3: / Line 3: @@
 <StructureSection load='1ck4' size='340' side='right'caption='[[1ck4]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ck4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. 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 [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1CK4 FirstGlance]. <br>
-</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://pdbe.org/1ck4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ck4 RCSB], [http://www.ebi.ac.uk/pdbsum/1ck4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ck4 ProSAT]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ck4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ck4 OCA], [https://pdbe.org/1ck4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ck4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ck4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ck4 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ITA1_RAT ITA1_RAT]] Integrin alpha-1/beta-1 is a receptor for laminin and collagen. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen.
+[[https://www.uniprot.org/uniprot/ITA1_RAT ITA1_RAT]] Integrin alpha-1/beta-1 is a receptor for laminin and collagen. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 29: / Line 29: @@
 ==See Also==
-*[[Integrin|Integrin]]
+*[[Integrin 3D structures|Integrin 3D structures]]
 == References ==
 <references/>

1ck4

From Proteopedia

Revision as of 10:43, 19 May 2021

CRYSTAL STRUCTURE OF RAT A1B1 INTEGRIN I-DOMAIN.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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