The relative influence of metal ion binding sites in the I-like domain and the interface with the hybrid domain on rolling and firm adhesion by integrin alpha4beta7.
Chen
JianFeng
J
The CBR Institute for Biomedical Research and Department of Pathology, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.
Takagi
Junichi
J
Xie
Can
C
Xiao
Tsan
T
Luo
Bing-Hao
BH
Springer
Timothy A
TA
D000595:Amino Acid Sequence; D001665:Binding Sites; D002118:Calcium / Q000737:chemistry; D002412:Cations; D002448:Cell Adhesion; D002460:Cell Line; D018076:DNA, Complementary / Q000378:metabolism; D005434:Flow Cytometry; D006031:Glycosylation; D006801:Humans; D047468:Immunoprecipitation; D016023:Integrins / Q000737:chemistry* / Q000378:metabolism; D007477:Ions; D008024:Ligands; D008274:Magnesium / Q000737:chemistry; D008345:Manganese / Q000737:chemistry; D008856:Microscopy, Fluorescence; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D011134:Polysaccharides / Q000737:chemistry; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D014162:Transfection
D002412:Cations; D018076:DNA, Complementary; D016023:Integrins; D007477:Ions; D008024:Ligands; D011134:Polysaccharides; C071777:integrin alpha4beta7; D008345:Manganese; D008274:Magnesium; D002118:Calcium