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1a8x

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{{Theoretical_model}}
{{Theoretical_model}}
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[[Image:1a8x.png|left|200px]]
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==HUMAN MAC-1 BETA-PROPELLER, THEORETICAL MODEL==
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<StructureSection load='1a8x' size='340' side='right'caption='[[1a8x]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A8X FirstGlance]. <br>
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</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=1a8x FirstGlance], [https://www.ebi.ac.uk/pdbsum/1a8x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a8x ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Integrins are large, heterodimeric surface molecules of wide importance in cell adhesion. The N-terminal half of all integrin alpha-subunits contains seven weak sequence repeats of approximately 60 amino acids that are important in ligand binding and have been predicted to fold cooperatively into a single beta-propeller domain with seven beta-sheets. We provide evidence supporting this model with a mouse mAb to human Mac-1 (alphaM beta2, CD11b/CD18). This antibody, CBRM1/20, binds to amino acid residues that are in different repeats and are 94 residues apart in the primary structure in the loop between strands 1 and 2 of beta-sheet 5 and in the loop between strands 3 and 4 of beta-sheet 6. The 1-2 loops of beta-sheets 5-7 in integrins have EF hand-like Ca2+-binding motifs. CBRM1/20 binds to Mac-1 in the presence of Ca2+ or Sr2+ with an EC50 of 0.2 mM. Mg2+ or Mn2+ cannot substitute. Antibodies to other epitopes on the Mac-1 beta-propeller domain bind in the absence of calcium. mAb CBRM1/20 does not block ligand binding. Thus, the region on the lower surface of the beta-propeller domain to which mAb CBRM1/20 binds does not bind ligand and, furthermore, cannot bind other integrin domains, such as those of the beta-subunit.
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{{STRUCTURE_1a8x| PDB=1a8x | SCENE= }}
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Experimental support for a beta-propeller domain in integrin alpha-subunits and a calcium binding site on its lower surface.,Oxvig C, Springer TA Proc Natl Acad Sci U S A. 1998 Apr 28;95(9):4870-5. PMID:9560195<ref>PMID:9560195</ref>
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===HUMAN MAC-1 BETA-PROPELLER, THEORETICAL MODEL===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_9560195}}
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<div class="pdbe-citations 1a8x" style="background-color:#fffaf0;"></div>
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:009560195</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
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[[Category: Theoretical Model]]
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[[Category: Large Structures]]
[[Category: Oxvig, C]]
[[Category: Oxvig, C]]
[[Category: Springer, T A]]
[[Category: Springer, T A]]

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

HUMAN MAC-1 BETA-PROPELLER, THEORETICAL MODEL

PDB ID 1a8x

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