Tailoring of Integrin Ligands: Probing the Charge Capability of the Metal Ion-Dependent Adhesion Site

2012 ◽  
Vol 55 (2) ◽  
pp. 871-882 ◽  
Author(s):  
Markus Bollinger ◽  
Florian Manzenrieder ◽  
Roman Kolb ◽  
Alexander Bochen ◽  
Stefanie Neubauer ◽  
...  
Keyword(s):  
Metal Ion ◽  
Integrin Ligands ◽  
Adhesion Site

scholarly journals “RKKH” Peptides from the Snake Venom Metalloproteinase ofBothrops jararacaBind Near the Metal Ion-dependent Adhesion Site of the Human Integrin α2I-domain

1999 ◽  
Vol 274 (44) ◽  
pp. 31493-31505 ◽  
Author(s):  
Olli Pentikäinen ◽  
Anna-Marja Hoffrén ◽  
Johanna Ivaska ◽  
Jarmo Käpylä ◽  
Tommi Nyrönen ◽  
...  
Keyword(s):  
Snake Venom ◽  
Metal Ion ◽  
Snake Venom Metalloproteinase ◽  
Human Integrin ◽  
Adhesion Site

scholarly journals Solvent-accessible Residues on the Metal Ion-dependent Adhesion Site Face of Integrin CR3 Mediate Its Binding to the Neutrophil Inhibitory Factor

1996 ◽  
Vol 271 (27) ◽  
pp. 15858-15861 ◽  
Author(s):  
Philippe Rieu ◽  
Takashi Sugimori ◽  
Diana L. Griffith ◽  
M. Amin Arnaout
Keyword(s):  
Metal Ion ◽  
Inhibitory Factor ◽  
Adhesion Site

scholarly journals Characterization of a Conformationally Sensitive Murine Monoclonal Antibody Directed to the Metal Ion-Dependent Adhesion Site Face of Integrin CD11b

2002 ◽  
Vol 168 (3) ◽  
pp. 1219-1225 ◽  
Author(s):  
Rui Li ◽  
Ikuko Haruta ◽  
Philippe Rieu ◽  
Takashi Sugimori ◽  
Jian-Ping Xiong ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Metal Ion ◽  
Murine Monoclonal Antibody ◽  
Adhesion Site

scholarly journals Variation in One Residue Associated with the Metal Ion-Dependent Adhesion Site Regulates αIIbβ3 Integrin Ligand Binding Affinity

PLoS ONE ◽  
2013 ◽  
Vol 8 (10) ◽  
pp. e76793 ◽  
Author(s):  
Joel Raborn ◽  
Ting Fu ◽  
Xue Wu ◽  
Zhilong Xiu ◽  
Guohui Li ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Binding Affinity ◽  
Metal Ion ◽  
Integrin Ligand ◽  
Αiibβ3 Integrin ◽  
Adhesion Site

scholarly journals Evidence That the Integrin β3 and β5 Subunits Contain a Metal Ion-dependent Adhesion Site-like Motif but Lack an I Domain

1997 ◽  
Vol 272 (22) ◽  
pp. 14236-14243 ◽  
Author(s):  
Emme C. K. Lin ◽  
Boris I. Ratnikov ◽  
Pamela M. Tsai ◽  
E. Rosalie Gonzalez ◽  
Shawn McDonald ◽  
...  
Keyword(s):  
Metal Ion ◽  
Integrin Β3 ◽  
Adhesion Site

scholarly journals Complete integrin headpiece opening in eight steps

2013 ◽  
Vol 201 (7) ◽  
pp. 1053-1068 ◽  
Author(s):  
Jieqing Zhu ◽  
Jianghai Zhu ◽  
Timothy A. Springer
Keyword(s):  
Metal Ion ◽  
Thermodynamic Cycle ◽  
Energetic Cost ◽  
Side Chain ◽  
Ligand Binding Site ◽  
Rgd Peptides ◽  
Hybrid Domain ◽  
Binding Groove ◽  
Αiibβ3 Integrin ◽  
Adhesion Site

Carefully soaking crystals with Arg-Gly-Asp (RGD) peptides, we captured eight distinct RGD-bound conformations of the αIIbβ3 integrin headpiece. Starting from the closed βI domain conformation, we saw six intermediate βI conformations and finally the fully open βI with the hybrid domain swung out in the crystal lattice. The β1-α1 backbone that hydrogen bonds to the Asp side chain of RGD was the first element to move followed by adjacent to metal ion-dependent adhesion site Ca2+, α1 helix, α1’ helix, β6-α7 loop, α7 helix, and hybrid domain. We define in atomic detail how conformational change was transmitted over long distances in integrins, 40 Å from the ligand binding site to the opposite end of the βI domain and 80 Å to the far end of the hybrid domain. During these movements, RGD slid in its binding groove toward αIIb, and its Arg side chain became ordered. RGD concentration requirements in soaking suggested a >200-fold higher affinity after opening. The thermodynamic cycle shows how higher affinity pays the energetic cost of opening.

scholarly journals Assessing Metal Ion Preference for the Metal Ion-Dependent Adhesion Site (MIDAS) of Platelet Integrin αIIbβ3

2013 ◽  
Vol 104 (2) ◽  
pp. 608a-609a
Author(s):  
Ana Negri ◽  
Ernesto E. Borrero ◽  
Davide Provasi ◽  
Barry S. Coller ◽  
Marta Filizola
Keyword(s):  
Metal Ion ◽  
Integrin Αiibβ3 ◽  
Adhesion Site
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