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The Chlamydial Porin (CP) Family [Function: Non-specific channels] Seed alignment | Full alignment in OMPdb

The Chlamydial Major Outer Membrane Protein (MOMP), functions to permit the diffusion of solutes through the intrareticular body membrane. MOMP is predicted to form a beta barrel, with 4 highly variable and immunogenic extracellular loops that determine the different serotypes. The four variable loops are not required for pore formation but rather serve in the modification of the channel function. 7 cysteines are found conserved in these loops, and disulfide bonds are formed between Cys(48)-Cys(55), Cys(201)-Cys(203), whereas Cys(51), Cys(136), Cys(226), and Cys(351), are free cysteines and, therefore, could potentially form disulfide-linked complexes with other MOMPs or other membrane components.

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Literature references

Characterization of the disulfide bonds and free cysteine residues of the Chlamydia trachomatis mouse pneumonitis major outer membrane protein
Biochemistry. 2005 Apr 26;44(16):6250-6. doi: 10.1021/bi047775v.
PMID: 15835913

Surface expression, single-channel analysis and membrane topology of recombinant Chlamydia trachomatis Major Outer Membrane Protein
BMC Microbiol. 2005 Jan 26;5:5. doi: 10.1186/1471-2180-5-5.
PMID: 15673471

Prediction of the membrane-spanning beta-strands of the major outer membrane protein of Chlamydia
Protein Sci. 2002 Jul;11(7):1854-61. doi: 10.1110/ps.3650102.
PMID: 12070338

Mutagenesis and functional reconstitution of chlamydial major outer membrane proteins: VS4 domains are not required for pore formation but modify channel function
Infect Immun. 2001 Mar;69(3):1671-8. doi: 10.1128/IAI.69.3.1671-1678.2001.
PMID: 11179342

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