 | This article provides insufficient context for those unfamiliar with the subject. Please help improve the article by providing more context for the reader. (April 2019) (Learn how and when to remove this message) |
| PAN_1 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 solution structure of a pan module from eimeria tenella | |||||||||
| Identifiers | |||||||||
| Symbol | PAN_1 | ||||||||
| Pfam | PF00024 | ||||||||
| Pfam clan | CL0168 | ||||||||
| InterPro | IPR003014 | ||||||||
| PROSITE | PDOC00376 | ||||||||
| SCOP2 | 1bht / SCOPe / SUPFAM | ||||||||
| |||||||||
PAN domains have significant functional versatility fulfilling diverse biological roles by mediating protein-protein and protein-carbohydrate interactions. These domains contain a hair-pin loop like structure, similar to that found in knottins but with a different pattern of disulfide bonds.
It has been shown that the N-terminal domains of members of the plasminogen/hepatocyte growth factor family, the apple domains of the plasma prekallikrein/coagulation factor XI family, and domains of various nematode proteins belong to the same module superfamily, the PAN module. The PAN domain contains a conserved core of three disulfide bridges. In some members of the family there is an additional fourth disulfide bridge that links the N- and C-termini of the domain.
The apple domain, as well as other examples of the PAN domain, consists of 7 β-strands that fold into a curved antiparallel sheet cradling an α-helix. Two disulfide bonds lock the helix onto the central β4 and β5 strands, whereas a third connects the N- and C-termini of the domain. In the apple domain, the β4-β5 loop and β5-β6 crossover loop generate a small pocket on the opposite side of the sheet from the α-helix.
In native plasminogen the PAN domain is associated with five kringle domains. The interactions between the PAN domain and the kringles play a critical role in stabilising the quaternary complex of the native plasminogen;
References
- ^ Tordai H, Bányai L, Patthy L (November 1999). "The PAN module: the N-terminal domains of plasminogen and hepatocyte growth factor are homologous with the apple domains of the prekallikrein family and with a novel domain found in numerous nematode proteins". FEBS Lett. 461 (1–2): 63–7. Bibcode:1999FEBSL.461...63T. doi:10.1016/s0014-5793(99)01416-7. PMID 10561497. S2CID 29929643.
- Emsley J, McEwan PA, Gailani D (Apr 2010). "Structure and function of factor XI". Blood. 115 (13): 2569–77. doi:10.1182/blood-2009-09-199182. PMC 4828079. PMID 20110423.
- Xue Y, Bodin C, Olsson K (2012). "Crystal structure of the native plasminogen reveals an activation-resistant compact conformation". J Thromb Haemost. 10 (7): 1385–96. doi:10.1111/j.1538-7836.2012.04765.x. PMID 22540246.
 | This protein-related article is a stub. You can help Misplaced Pages by expanding it. |