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1qc5

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[[Image:1qc5.gif|left|200px]]<br />
 
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<applet load="1qc5" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qc5, resolution 2.000&Aring;" />
 
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'''I DOMAIN FROM INTEGRIN ALPHA1-BETA1'''<br />
 
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==Overview==
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==I Domain from Integrin Alpha1-Beta1==
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Most mammalian cells and some pathogenic bacteria are capable of adhering, to collagenous substrates in processes mediated by specific cell surface, adherence molecules. Crystal structures of collagen-binding regions of the, human integrin alpha(2)beta(1) and a Staphylococcus aureus adhesin reveal, a "trench" on the surface of both of these proteins. This trench can, accommodate a collagen triple-helical structure and presumably represents, the ligand-binding site (Emsley, J., King, S. L., Bergelson, J. M., and, Liddington, R. C. (1997) J. Biol. Chem. 272, 28512-28517; Symersky, J., Patti, J. M., Carson, M., House-Pompeo, K., Teale, M., Moore, D., Jin, L., Schneider, A., DeLucas, L. J., Hook, M., and Narayana, S. V. L. (1997), Nat. Struct. Biol. 4, 833-838). We report here the crystal structure of, the alpha subunit I domain from the alpha(1)beta(1) integrin. This, collagen-binding protein also contains a trench on one face in which the, collagen triple helix may be docked. Furthermore, we compare the, collagen-binding mechanisms of the human alpha(1) integrin I domain and, the A domain from the S. aureus collagen adhesin, Cna. Although the S., aureus and human proteins have unrelated amino acid sequences, secondary, structure composition, and cation requirements for effective ligand, binding, both proteins bind at multiple sites within one collagen, molecule, with the sites in collagen varying in their affinity for the, adherence molecule. We propose that (i) these evolutionarily dissimilar, adherence proteins recognize collagen via similar mechanisms, (ii) the, multisite, multiclass protein/ligand interactions observed in these two, systems result from a binding-site trench, and (iii) this unusual binding, mechanism may be thematic for proteins binding extended, rigid ligands, that contain repeating structural motifs.
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<StructureSection load='1qc5' size='340' side='right'caption='[[1qc5]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1qc5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QC5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QC5 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qc5 OCA], [https://pdbe.org/1qc5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qc5 RCSB], [https://www.ebi.ac.uk/pdbsum/1qc5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qc5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ITA1_HUMAN ITA1_HUMAN] 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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qc/1qc5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qc5 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1QC5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: MGA. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QC5 OCA].
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*[[Integrin 3D structures|Integrin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Trench-shaped binding sites promote multiple classes of interactions between collagen and the adherence receptors, alpha(1)beta(1) integrin and Staphylococcus aureus cna MSCRAMM., Rich RL, Deivanayagam CC, Owens RT, Carson M, Hook A, Moore D, Symersky J, Yang VW, Narayana SV, Hook M, J Biol Chem. 1999 Aug 27;274(35):24906-13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10455165 10455165]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Deivanayagam, C.C.]]
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[[Category: Deivanayagam CC]]
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[[Category: Narayana, S.V.]]
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[[Category: Narayana SV]]
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[[Category: MG]]
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[[Category: cell adhesion]]
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[[Category: integrin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 16:59:41 2007''
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Current revision

I Domain from Integrin Alpha1-Beta1

PDB ID 1qc5

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