3GHG
Crystal Structure of Human Fibrinogen
Summary for 3GHG
| Entry DOI | 10.2210/pdb3ghg/pdb |
| Related | 1DEQ 1FZC 1M1J 2A45 |
| Descriptor | Fibrinogen alpha chain, Fibrinogen beta chain, Fibrinogen gamma chain, ... (9 entities in total) |
| Functional Keywords | triple-stranded coiled coil, beta sheets, alpha helices, amyloid, amyloidosis, blood coagulation, disease mutation, glycoprotein, phosphoprotein, secreted, pyrrolidone carboxylic acid, sulfation, blood clotting |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 20 |
| Total formula weight | 651387.77 |
| Authors | Doolittle, R.F.,Kollman, J.M.,Sawaya, M.R.,Pandi, L.,Riley, M. (deposition date: 2009-03-03, release date: 2009-05-19, Last modification date: 2024-11-06) |
| Primary citation | Kollman, J.M.,Pandi, L.,Sawaya, M.R.,Riley, M.,Doolittle, R.F. Crystal structure of human fibrinogen. Biochemistry, 48:3877-3886, 2009 Cited by PubMed Abstract: A crystal structure of human fibrinogen has been determined at approximately 3.3 A resolution. The protein was purified from human blood plasma, first by a cold ethanol precipitation procedure and then by stepwise chromatography on DEAE-cellulose. A product was obtained that was homogeneous on SDS-polyacrylamide gels. Nonetheless, when individual crystals used for X-ray diffraction were examined by SDS gel electrophoresis after data collection, two species of alpha chain were present, indicating that some proteolysis had occurred during the course of operations. Amino-terminal sequencing on post-X-ray crystals showed mostly intact native alpha- and gamma-chain sequences (the native beta chain is blocked). The overall structure differs from that of a native fibrinogen from chicken blood and those reported for a partially proteolyzed bovine fibrinogen in the nature of twist in the coiled-coil regions, likely due to weak forces imparted by unique crystal packing. As such, the structure adds to the inventory of possible conformations that may occur in solution. Other features include a novel interface with an antiparallel arrangement of beta chains and a unique tangential association of coiled coils from neighboring molecules. The carbohydrate groups attached to beta chains are unusually prominent, the full sweep of 11 sugar residues being positioned. As was the case for native chicken fibrinogen, no resolvable electron density could be associated with alphaC domains. PubMed: 19296670DOI: 10.1021/bi802205g PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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