1RHP
CRYSTAL STRUCTURE OF RECOMBINANT HUMAN PLATELET FACTOR 4
Summary for 1RHP
| Entry DOI | 10.2210/pdb1rhp/pdb |
| Descriptor | PLATELET FACTOR 4 (2 entities in total) |
| Functional Keywords | platelet factor |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted: P02776 |
| Total number of polymer chains | 4 |
| Total formula weight | 31128.78 |
| Authors | |
| Primary citation | Zhang, X.,Chen, L.,Bancroft, D.P.,Lai, C.K.,Maione, T.E. Crystal structure of recombinant human platelet factor 4. Biochemistry, 33:8361-8366, 1994 Cited by PubMed Abstract: The crystal structure of human platelet factor 4 (PF4) has been solved to a resolution of 2.4 A by molecular replacement and refined to an R-factor of 24.1%. The structure consists of four polypeptide chains which form a tetrameric unit. N-terminal residues, previously defined as a random coil or extended loop region, form antiparallel beta-sheet-like structures that form noncovalent associations between dimers. These antiparallel beta-sheet-like structures are positioned lateral to the beta-bilayer motif and stabilize the tetrameric unit. A positively charged ring of lysine and arginine side chains encircles the PF4 tetramer sphere, presenting multiple potential sites and orientations for heparin binding. The electrostatic interactions of multiply charged amino acid side chains and hydrogen bonding interactions at the AB/CD dimer interface serve to stabilize the tetrameric structure further. PubMed: 8031770DOI: 10.1021/bi00193a025 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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