Bowman–Birk protease inhibitor
| Bowman–Birk leg | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 High resolution structure of barley Bowman-Birk protease inhibitor | |||||||||
| Identifiers | |||||||||
| Symbol | Bowman-Birk_leg | ||||||||
| Pfam | PF00228 | ||||||||
| InterPro | IPR000877 | ||||||||
| PROSITE | PDOC00253 | ||||||||
| SCOP | 1pi2 | ||||||||
| SUPERFAMILY | 1pi2 | ||||||||
| CDD | cd00023 | ||||||||
| |||||||||
In molecular biology, Bowman–Birk protease inhibitor family of proteins consist of eukaryotic proteinase inhibitors, belonging to MEROPS inhibitor family I12, clan IF. They mainly inhibit serine peptidases of the S1 family, but also inhibit S3 peptidases.[1][2]
Members of this family have a duplicated structure and generally possess two distinct inhibitory sites. These inhibitors are primarily found in plants and in particular in the seeds of legumes, as well as in cereal grains.[3] In cereals, they exist in two forms, one of which is a duplication of the basic structure.[4] Proteins of the Bowman–Birk inhibitor family of serine proteinase inhibitors interact with the enzymes they inhibit via an exposed surface loop that adopts the canonical proteinase inhibitory conformation. The resulting noncovalent complex renders the proteinase inactive. This inhibition mechanism is common for the majority of serine proteinase inhibitor proteins, and many analogous examples are known. A particular feature of the Bowman–Birk inhibitor protein, however, is that the interacting loop is a particularly well-defined, disulfide-linked, short beta-sheet region.[5][6][7]
References
- ↑ Rawlings ND, Tolle DP, Barrett AJ (March 2004). "Evolutionary families of peptidase inhibitors". Biochem. J. 378 (Pt 3): 705â16. doi:10.1042/BJ20031825. PMC 1224039. PMID 14705960. C1 control character in
|pages=at position 5 (help) - ↑ Laskowski M, Kato I (1980). "Protein inhibitors of proteinases". Annu. Rev. Biochem. 49: 593â626. doi:10.1146/annurev.bi.49.070180.003113. PMID 6996568. C1 control character in
|pages=at position 5 (help) - ↑ Birk, Y (February 1985). "The Bowman-Birk inhibitor. Trypsin- and chymotrypsin-inhibitor from soybeans.". International journal of peptide and protein research 25 (2): 113–31. doi:10.1111/j.1399-3011.1985.tb02155.x. PMID 3886572.
- ↑ Tashiro M, Hashino K, Shiozaki M, Ibuki F, Maki Z (August 1987). "The complete amino acid sequence of rice bran trypsin inhibitor". J. Biochem. 102 (2): 297â306. PMID 3667571. C1 control character in
|pages=at position 5 (help) - ↑ McBride JD, Leatherbarrow RJ (July 2001). "Synthetic peptide mimics of the Bowman-Birk inhibitor protein". Curr. Med. Chem. 8 (8): 909–17. doi:10.2174/0929867013372832. PMID 11375759.
- ↑ McBride JD, Watson EM, Brauer AB, Jaulent AM, Leatherbarrow RJ (2002). "Peptide mimics of the Bowman-Birk inhibitor reactive site loop". Biopolymers 66 (2): 79â92. doi:10.1002/bip.10228. PMID 12325158. C1 control character in
|pages=at position 4 (help) - ↑ Brauer AB, Nievo M, McBride JD, Leatherbarrow RJ (April 2003). "The structural basis of a conserved P2 threonine in canonical serine proteinase inhibitors". J. Biomol. Struct. Dyn. 20 (5): 645â56. doi:10.1080/07391102.2003.10506881. PMID 12643767. C1 control character in
|pages=at position 5 (help)
External links
This article incorporates text from the public domain Pfam and InterPro IPR000877