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.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Zhang X,Chen L,Bancroft DP,Lai CK,Maione TEdoi
10.1021/bi00193a025subject
Has Abstractpub_date
1994-07-12 00:00:00pages
8361-6issue
27eissn
0006-2960issn
1520-4995journal_volume
33pub_type
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