1DGU
HOMOLOGY-BASED MODEL OF CALCIUM-SATURATED CIB (CALCIUM-AND INTEGRIN-BINDING PROTEIN)
Summary for 1DGU
| Entry DOI | 10.2210/pdb1dgu/pdb |
| Related | 1DGV |
| Descriptor | CALCIUM-SATURATED CIB (1 entity in total) |
| Functional Keywords | helical, ef-hands, blood clotting |
| Biological source | Homo sapiens (human) |
| Cellular location | Membrane; Lipid-anchor: Q99828 |
| Total number of polymer chains | 1 |
| Total formula weight | 20980.49 |
| Authors | Hwang, P.M.,Vogel, H.J. (deposition date: 1999-11-25, release date: 1999-12-08, Last modification date: 2024-05-22) |
| Primary citation | Hwang, P.M.,Vogel, H.J. Structures of the platelet calcium- and integrin-binding protein and the alphaIIb-integrin cytoplasmic domain suggest a mechanism for calcium-regulated recognition; homology modelling and NMR studies. J.Mol.Recog., 13:83-92, 2000 Cited by PubMed Abstract: Calcium- and integrin-binding protein (CIB) binds to the 20-residue alphaIIb cytoplasmic domain of platelet alphaIIbbeta3 integrin. Amino acid sequence similarities with calmodulin (CaM) and calcineurin B (CnB) allowed the construction of homology-based models of calcium-saturated CIB as well as apo-CIB. In addition, the solution structure of the alphaIIb cytoplasmic domain in 45% aqueous trifluoroethanol was solved by conventional two-dimensional NMR methods. The models indicate that the N-terminal domain of CIB possesses a number of positively charged residues in its binding site that could interact with the acidic carboxy-terminal LEEDDEEGE sequence of alphaIIb. The C-terminal domain of CIB seems well-suited to bind the sequence WKVGFFKR, which forms a well-structured alpha helix; this is analogous to calmodulin and calcineurin B, which also bind alpha helices. Similarities between the C-terminal domains of CIB and calmodulin suggest that binding of CIB to the cytoplasmic domain of alphaIIb may be affected by fluctuations in the intracellular calcium concentration. PubMed: 10822252DOI: 10.1002/(SICI)1099-1352(200003/04)13:2<83::AID-JMR491>3.3.CO;2-1 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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