NLProt output:
red             protein names
blue            species/organism
green           tissue/cell types
TXT-POS         Text position of the first word of the name (note any non-word character such as "." count as one word)
SCORE           Score of NLProt (protein name if > 0)
METHOD          SVM = found by SVM
                projected = found by SVM but at another position than this one
                inherited = similar to an already found name (e.g. CCR4 and CCR5)
                dictionary = strong dictionary entry (long name in protein dictionary)
DB-ID(S)        List of database identifiers for proteins with this name (in database specified in query)



ID: 15128297
Actin-binding domain of mouse plectin. Plectin, a large and widely expressed cytolinker protein, is composed of several subdomains that harbor binding sites for a variety of different interaction partners. A canonical actin-binding domain (ABD) comprising two calponin homology domains (CH1 and CH2) is located in proximity to its amino terminus. However, the ABD of plectin is unique among actin-binding proteins as it is expressed in the form of distinct, plectin isoform-specific versions. We have determined the three-dimensional structure of two distinct crystalline forms of one of its ABD versions (pleABD/2alpha) from mouse, to a resolution of 1.95 and 2.0 A. Comparison of pleABD/2alpha with the ABDs of fimbrin and utrophin revealed structural similarity between plectin and fimbrin, although the proteins share only low sequence identity. In fact, pleABD/2alpha has been found to have the same compact fold as the human plectin ABD and the fimbrin ABD, differing from the open conformation described for the ABDs of utrophin and dystrophin. Plectin harbors a specific binding site for intermediate filaments of various types within its carboxy-terminal R5 repeat domain. Our experiments revealed an additional vimentin-binding site of plectin, residing within the CH1 subdomain of its ABD. We show that vimentin binds to this site via the amino-terminal part of its rod domain. This additional amino-terminal intermediate filament protein binding site of plectin may have a function in intermediate filament dynamics and assembly, rather than in linking and stabilizing intermediate filament networks.


The following protein names could be found by NLProt:

NAME ORGANISM TXT-POS SCORE METHOD DB-ID(S)
plectinmouse 51.464SVMQ923J2 (100%)
Plectinmouse 71.226SVMQ923J2 (100%)
calponinmouse 431.125SVMCLP1_MOUSE (47%)
CH1mouse 471.380inheritedBAC1_MOUSE (1%)
CH2mouse 491.380SVMBAC2_MOUSE (1%)
plectinmouse 651.387SVMQ923J2 (100%)
plectinmouse 810.650SVMQ923J2 (100%)
ABDsmouse 1220.161projectedno ID found
fimbrinmouse 1241.459SVMGS27_MOUSE (86%)
utrophinmouse 1261.283SVMQ8BJ20 (100%)
plectinmouse 1311.266SVMQ923J2 (100%)
fimbrinhuman 1331.367SVMGS27_HUMAN (86%)
plectinhuman 1600.797SVMPLE1_HUMAN (88%)
fimbrinhuman 1640.749SVMGS27_HUMAN (86%)
ABDshuman 1750.161SVMno ID found
utrophinhuman 1771.453SVMUTRO_HUMAN (100%)
dystrophinhuman 1791.491SVMDMD_HUMAN (100%)
Plectinhuman 1810.700SVMPLE1_HUMAN (81%)
vimentinhuman 2051.153projectedVIME_HUMAN (100%)
plectinhuman 2081.418SVMPLE1_HUMAN (88%)
CH1human 2131.380inheritedQ9UL04 (100%)
vimentinhuman 2221.153SVMVIME_HUMAN (100%)
plectinhuman 2451.319SVMPLE1_HUMAN (88%)


// END OF NLPROT OUTPUT

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