| General information | | DisProt: | DP00137 | | Name: | Hirudin variant-1 | | Synonym(s): | HIRV1_HIRME
Hirudin-1
Hirudin-I
Lepirudin
| | First appeared in release: | Release 1.0 (08/01/2003) | | UniProt: | P01050 | | UniGene: | | | SwissProt: | HIRV1_HIRME | | TrEMBL: | | | NCBI (GI): | 124981 | | Source organism: | Hirudo medicinalis (Medicinal leech) | | Sequence length: | 65 | | Percent disordered: | 25% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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VVYTDCTESG QNLCLCEGSN VCGQGNKCIL GSDGEKNQCV TGEGTPKPQS HNDGDFEEIP - 60
EEYLQ
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| Functional narrative |
Hirudin variant-1 is a thrombin-specific protease inhibitor. This protein interacts and targets alpha-thrombin to negate its ability to cleave fibrinogen. Because of this, Hirudin variant-1 is an excellent anti-coagulant which is generally secreted by cells. As a member of the Hirudin family of proteins, this protein is utilized in many medications to treat diseases such as heparin-induced thrombocytopenia (HIT). Although this protein does contain a disordered C-terminal tail, the function of this disordered region has yet to be determined.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered - Extended | | Name: | C-Terminal Tail | | Location: | 50 - 65 | | Length: | 16 | | Region sequence: |
SHNDGDFEEIPEEYLQ | | Modification type: | Native
| | PDB: | 1HRT:A, 2HIR:A, 5HIR:A | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- Nuclear magnetic resonance (NMR) (300 K; D20; H20)
| References:
- Dodt J, Schmitz T, Schafer T, Bergmann C. "Expression, secretion and processing of hirudin in E. coli using the alkaline phosphatase signal sequence." FEBS Lett. 1986; 202(2): 373-7. PubMed: 3013692
- Folkers PJ, Clore GM, Driscoll PC, Dodt J, Kohler S, Gronenborn AM. "Solution structure of recombinant hirudin and the Lys-47----Glu mutant: a nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing study." Biochemistry. 1989; 28(6): 2601-17. PubMed: 2567183
| Comments:
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