| General information | | DisProt: | DP00746 | | Name: | PfEMP1 variant 1 of strain MC | | Synonym(s): | Q25733_PLAFA
Erythrocyte membrane protein-1
EMP1
PfEMP1 variant 1 of strain Malayan Camp (MC)
| | First appeared in release: | Release 6.02 (05/24/2013) | | UniProt: | Q25733 | | UniGene: | | | SwissProt: | Q25733_PLAFA | | TrEMBL: | | | NCBI (GI): | | | Source organism: | Plasmodium falciparum | | Sequence length: | 2924 | | Percent disordered: | 1% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MGGGNGGGGT KDKDAKHALD RIGEEVYKEK VENDAEKYKK ALKGNLQEAK GIGELASSPN - 60
PCKLVEDYYN NRLKRKRYPC ANRQTVRFSD EYGGQCTFNR IKDSENNDNS IGACAPYRRL - 120
HLCDYNLEKM GKTSTTKHDL LLDVCMAAKY EGDSIKTHYT KHELTNPDTK SQLCTILARS - 180
FADIGDIVRG KDLYLGYDDK EKDERKKLEN NLIEIFKKIH ENLGTQDAKD HYKKDEENYY - 240
QLREDWWTAN RSTVWKAITC HAGESDKYFR KTCCSGEWTD DKCRCKDEEG KNETNEVPTY - 300
FDYVPQYLRW FEEWAEDFCR KRKKKIENAI KNCRGEKGNE RYCDLNGYNC EETARGAEIF - 360
VKGDDCHKCS VACDRFVKWI DNQRKEFDKQ KKKYDEEINK THGTTITTGN GKINNLYVGH - 420
FYKILKKYYP TVDKSLQKLN DEAICKKPPN VGNEKASTVD FNNEVNTTFS HTTYCEACPW - 480
CGAQKEKNGG GWKAKEKSCA KKKERIFNKE NSTDIKILTP EKGRSKTLEK LKTFCKDGQK - 540
IKNDIWKCHY DDNGTDDQTD DSNDCVLGDW GNLTKEDKIM SYNAFFWMWV HDMLIDSIKW - 600
RDEHGRCINK DKGKTCIKGC NKKCICFQKW VEQKKTEWGK IKDHFRKQKD IPKDWTHDDF - 660
LQTLLMKDLL LEIIQDTYGD ANEIKRIEAL LEQAGVGGID FAALAGLYTK GFVAEKDTTI - 720
DKLLQHEQKE ADKCLKTHTD DTCPPQEDRS VARSESATVP SPPADPKATE EVDANASSDD - 780
EDDFEEEEEE EEDEGEEEAE EVQEEKTDES ATEAVAPSPP GTTQDGVKPA SQEDDVKVCS - 840
IVDKALKGKL DDACTLKYGK TAPTSWKCIP SGNNTTTEST TKPGAAGTPS GKDTGSICVP - 900
PRRRKLYVGK LHDWAGGETT EAKSQETSGG QKTPSGNESS PSEKLPQGPT PETTKETPES - 960
SLLHAFVSPP RLRRFLPWHK FKEQWKAQHG AGATGQQTII GTLDGGGEET PDKLLKTGHI - 1020
PPDFLRQMFY TLGDYRDILV GNTDIVVHTS GNKEDMQIME AIQKKIEQIL PTSGSSPSPP - 1080
RVTQTQHSVE NPRKTWWNEN GKKIWEGMVC ALTYNTDTPS GTAPTQIQEV RTKLRDENSK - 1140
NPKIPQYKYD QVKLDDTSDA KTTGSPVPSG EKITPLTDFI SRPPYFRYLE EWGETFCKER - 1200
KKRLEKIKEE CRGDRTGHEH CSGDGYDCTR TDADRNDKFV DLNCRDCHIQ CRKYRKWIDI - 1260
KFDEYHKQEK KYQGEYDKLT KDKSSGGDNN CCKDIEKHKS AAVFLKELKH CKNGQTSENK - 1320
GNQEDQLNKL DFDKIPQTFS PSTYCKACPV YGVNCNGNKR GRGGTNGCTT NNEPENKEND - 1380
KGAASTISIL INDGSTNGAT NGTTGTTDET LKECSDKYAF FKGLRKQEWT CQKKYGVNQC - 1440
NLTNRVNDTY FDKDIVFNEF FQRWLRYFVH DYNILKHKID PCIKKEKQDK TEHKCINGCN - 1500
IKCECVRKWL EIKGNEWGNI KKHYNINSND DKETIAYNVK SYFVDQGLFD TDYKKAQKVV - 1560
EDEKERKKIW GCTGHDECSE KEKEENKNFI TNLISELQDK ITSCQNKHNP NGKTACDPFP - 1620
SPTPEETDPL DDDTPDPLDD DQHTEQPKFC PPPPPPMTCV EKIAKELRVE AEGKINNELK - 1680
GNGKDFNGKC NNVKKKNGAV IGEESCKFEQ TYENSVNNIN NKCKDNQNER FKIGQKWNFK - 1740
YIGTIRKDLC IPPRREHMCL DDLSMLGRTT ISDSSALLKK IQEAAKSERD DIIRKLLEQN - 1800
SCDEHRICDA MKYSFADLGD IIRGRDLWNK NSKQKGLQKR LEYAFINIYN KLQNDKNKYE - 1860
KDRPKYLQLR SDWWDANRKH IWNAMTCNAP DDAKFLKKNP NDTSGSSSSK GIMTTHSNCG - 1920
YDKEPPDYDY IPQPFRWMQE WSESFCKLLN EEMEQFEKTC GECKKNSITC EDDRNGTNCE - 1980
NCKNQCEKYK KLIHNWKLGF DKYKEIYNEI YNNKDSKINS NEYFKKFLEK LKDKCKELNS - 2040
SDKCIDEATH CTKYKFSNSE NKNHNNYAFK NPPKEYEKAC KCDAPDPLDN CPKDSATYEK - 2100
ACNTLLPTKL CESKTFNNDD DSWDTSFVQT SPRDNTGVLV PPRRRQICLK NITTKLRSIE - 2160
KIDDFKAELM TSAYNEGKLL CELYKKDRDV TLQAMKYSFY DYGDIVKGTD LISTAPLDKL - 2220
KTKLNVLLKG DGTNEIKEDR GKWWTENRTR VWHAMLCGYK AAGGKIEERD CSLPDDNTHQ - 2280
FLRWFREWSE HFCAKRQKLF NEVKRECASA QCIIEYGTID PPVCEEACTQ YRDYITRKIQ - 2340
EYRLLNYQYN TNFNEKKAEV TKAPEYFNDK CNDKCNCLSK YIDIEKKWKN MYDSFDDNDL - 2400
KNKCICRQIK PKRPPKKVKP EEEHTPSEQD TPPPLPPKPD DLPPPAEEPF NRDILEKTIP - 2460
FGIALALGSI AFLFLKKKTK SSVGNLFQIL HIPKSDYDIP TKLSPNRYIP YTSGKYRGKR - 2520
YIYLEGDSGT DSGYTDHYSD ITSSSESEYE ELDINDIYVP GSPKYKTLIE VVLEPSGNNT - 2580
TASGKNTPSD TQNDIQNDGI PSSKITDNEW NTLKDEFISN MLQNEPNTEP NMLGYNVDNN - 2640
THPTTSRHNV EEKPFIMSIH DRDLYSGEEY SYNVNMVNND IPISARNGNY SGIDLINDSL - 2700
NSNKVDIYDE LLKRKENELF GTNHTKKNTS TNSVAKNTNT DPIHNQLNLF HTWLDRHRDM - 2760
CEKWDTNNKK EELLDKLKEE WNKDNNSGNI NPSGNTPPTS DIPSGKQSDI PSDNNIHSDI - 2820
PYVLNTDVSI QIHMDNPKPI NEFSNMDTYP NNSSMDTILE DLDKPFNEPY YYDVQDDIYY - 2880
DVHDHDTSTV DTNAMDEPSK VQIEMDVNTK LVKEKYPIAD LWDI
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| Functional narrative |
The erythrocyte membrane protein-1 (PfEMP1) family from the malaria parasite, Plasmodium falciparum, is expressed on the surface of infected human red blood cells. According to Klein et al (2008), the PfEMP1 proteins are "highly polymorphic and modular." Further, "(T)he binding of PfEMP1 molecules to human cell surface receptors mediates the adherence of infected red blood cells to human tissues. The sequences of the 60 PfEMP1 genes in each parasite genome vary greatly from parasite to parasite, yet the variant PfEMP1 proteins maintain receptor binding. Almost all parasites isolated directly from patients bind the human CD36 receptor." (Klein MM,et al. PLoS Pathog. 2008; 4(9): e1000147.)
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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 | | Name: | loop H1-H2 of MC179 peptide | | Location: | 605 - 618 | | Length: | 14 | | Region sequence: |
GRCINKDKGKTCIK | | Modification type: | Fragment
| | PDB: | 3C64:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Intraprotein interaction
| Detection methods:
- X-ray crystallography (298 K; pH: 4.2; NaCl 100 mM; PEG 400 27 %; Sodium citrate 50 mM)
| References:
- Klein MM, Gittis AG, Su HP, Makobongo MO, Moore JM, Singh S, Miller LH, Garboczi DN. "The cysteine-rich interdomain region from the highly variable plasmodium falciparum erythrocyte membrane protein-1 exhibits a conserved structure." PLoS Pathog.. 2008; 4(9): e1000147. PubMed: 18773118
| Comments:PDB structure 3C64 (Klein et al, 2008) represents a 179 aa peptide, MC179, part of the cysteine-rich interdomain region CIDR1-alpha. CIDR1-alpha is involved in binding to human CD36.
Klein et al describe the structure of MC179 as a 'V-shape' consisting of a three-helix bundle with three additional helices "between the H2 and H3 helices, in the order H1-H2-a-b-c-H3."
Conserved cysteines are located in disordered loop H1-H2, as well as at N-terminus of H2 and in disordered C-terminus of MC179.
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| Region 2 | | Type: | Disordered | | Name: | C-terminal loop of MC179 peptide | | Location: | 743 - 754 | | Length: | 12 | | Region sequence: |
CPPQEDRSVARS | | Modification type: | Fragment
| | PDB: | 3C64:A | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Intraprotein interaction
| Detection methods:
- X-ray crystallography (298 K; pH: 4.2; NaCl 100 mM; PEG 400 27 %; Sodium citrate 50 mM)
| References:
- Klein MM, Gittis AG, Su HP, Makobongo MO, Moore JM, Singh S, Miller LH, Garboczi DN. "The cysteine-rich interdomain region from the highly variable plasmodium falciparum erythrocyte membrane protein-1 exhibits a conserved structure." PLoS Pathog.. 2008; 4(9): e1000147. PubMed: 18773118
| Comments:PDB structure 3C64 (Klein et al, 2008) represents a 179 aa peptide, MC179, part of the cysteine-rich interdomain region CIDR1-alpha. CIDR1-alpha is involved in binding to human CD36.
Klein et al describe the structure of MC179 as a 'V-shape' consisting of a three-helix bundle with three additional helices "between the H2 and H3 helices, in the order H1-H2-a-b-c-H3."
Conserved cysteines are located in disordered loop H1-H2, as well as at N-terminus of H2 and in disordered C-terminus of MC179.
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| References |
- Klein MM, Gittis AG, Su HP, Makobongo MO, Moore JM, Singh S, Miller LH, Garboczi DN. "The cysteine-rich interdomain region from the highly variable plasmodium falciparum erythrocyte membrane protein-1 exhibits a conserved structure." PLoS Pathog.. 2008; 4(9): e1000147. PubMed: 18773118
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