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1a8x
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(New page: '''Theoretical Model''' The entry 1A8X is a Theoretical Model titled 'HUMAN MAC-1 BETA-PROPELLER, THEORETICAL MODEL'. Category:Theoretical Model ''Page seeded by [http://oca.weizma...) |
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| - | + | {{Theoretical_model}} | |
| - | + | ==HUMAN MAC-1 BETA-PROPELLER, THEORETICAL MODEL== | |
| + | <StructureSection load='1a8x' size='340' side='right'caption='[[1a8x]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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> | ||
| + | </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> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1a8x" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Theoretical Model]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Oxvig, C]] | ||
| + | [[Category: Springer, T A]] | ||
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HUMAN MAC-1 BETA-PROPELLER, THEORETICAL MODEL
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