Struktur: Orthorhombic Form of Igg1 FAB Fragment (IN Complex With Antigenic Tubulin Peptide) Sharing Same FV As Iga

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Struktur

Orthorhombic Form of Igg1 FAB Fragment (IN Complex With Antigenic Tubulin Peptide) Sharing Same
FV as IGA

Biological Unit: trimeric; determined by author, and by software (PISA)


Interactions? Molecular Graphic ?

Molecules and interactions


Label Count Molecule Interactions
Proteins and interactions (3 molecules)
FAB Fragment of Immunoglobulin G1 Light  FAB Fragment of
Chain Immunoglobulin G1
Heavy Chain
1  Glycerin
 Peptide From Tubulin
Beta Chain
Show annotation ▼
FAB Fragment of Immunoglobulin G1 Heavy
Chain  FAB Fragment of
Immunoglobulin G1
Light Chain
1
 Peptide From Tubulin
Beta Chain

Show annotation ▼
 FAB Fragment of
Immunoglobulin G1
Peptide From Tubulin Beta Chain Heavy Chain
1  FAB Fragment of
Show annotation ▼ Immunoglobulin G1
Light Chain

Chemical and interactions (1 molecule)


Molecules and interactions
Label Count Molecule Interactions

 FAB Fragment of
Immunoglobulin G1
1
Light Chain

Glycerin

Protein

tubulin beta chain isoform e [Homo sapiens]


NCBI Reference Sequence: NP_001280145.1

Identical Proteins FASTA Graphics

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LOCUS NP_001280145 372 aa linear PRI 21-FEB-
2016
DEFINITION tubulin beta chain isoform e [Homo sapiens].
ACCESSION NP_001280145
VERSION NP_001280145.1 GI:645912984
DBSOURCE REFSEQ: accession NM_001293216.1
KEYWORDS RefSeq.
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 372)
AUTHORS Laurin Y, Savarin P, Robert CH, Takahashi M, Eyer J, Prevost C
and
Sacquin-Mora S.
TITLE Investigating the Structural Variability and Binding Modes of the
Glioma Targeting NFL-TBS.40-63 Peptide on Tubulin
JOURNAL Biochemistry 54 (23), 3660-3669 (2015)
PUBMED 26016807
REMARK GeneRIF: Data suggest that, while lacking a stable structure,
NFL-TBS.40-63 peptide (a peptide derived from light neurofilament
protein) preferentially binds on a specific single site located
near C-terminal end of beta-tubulin.
REFERENCE 2 (residues 1 to 372)
AUTHORS Li X, Wang W, Wang J, Malovannaya A, Xi Y, Li W, Guerra R, Hawke
DH, Qin J and Chen J.
TITLE Proteomic analyses reveal distinct chromatin-associated and
soluble
transcription factor complexes
JOURNAL Mol. Syst. Biol. 11 (1), 775 (2015)
PUBMED 25609649
REMARK Publication Status: Online-Only
REFERENCE 3 (residues 1 to 372)
AUTHORS Reyniers L, Del Giudice MG, Civiero L, Belluzzi E, Lobbestael E,
Beilina A, Arrigoni G, Derua R, Waelkens E, Li Y, Crosio C,
Iaccarino C, Cookson MR, Baekelandt V, Greggio E and Taymans JM.
TITLE Differential protein-protein interactions of LRRK1 and LRRK2
indicate roles in distinct cellular signaling pathways
JOURNAL J. Neurochem. 131 (2), 239-250 (2014)
PUBMED 24947832
REFERENCE 4 (residues 1 to 372)
AUTHORS Tracy CM, Gray AJ, Cuellar J, Shaw TS, Howlett AC, Taylor RM,
Prince JT, Ahn NG, Valpuesta JM and Willardson BM.
TITLE Programmed cell death protein 5 interacts with the cytosolic
chaperonin containing tailless complex polypeptide 1 (CCT) to
regulate beta-tubulin folding
JOURNAL J. Biol. Chem. 289 (7), 4490-4502 (2014)
PUBMED 24375412
REFERENCE 5 (residues 1 to 372)
AUTHORS Yen TJ, Machlin PS and Cleveland DW.
TITLE Autoregulated instability of beta-tubulin mRNAs by recognition of
the nascent amino terminus of beta-tubulin
JOURNAL Nature 334 (6183), 580-585 (1988)
PUBMED 3405308
REFERENCE 6 (residues 1 to 372)
AUTHORS Wang,D., Villasante,A., Lewis,S.A. and Cowan,N.J.
TITLE The mammalian beta-tubulin repertoire: hematopoietic expression
of
a novel, heterologous beta-tubulin isotype
JOURNAL J. Cell Biol. 103 (5), 1903-1910 (1986)
PUBMED 3782288
REFERENCE 7 (residues 1 to 372)
AUTHORS Floyd-Smith,G., De Martinville,B. and Francke,U.
TITLE An expressed beta-tubulin gene, TUBB, is located on the short arm
of human chromosome 6 and two related sequences are dispersed on
chromosomes 8 and 13
JOURNAL Exp. Cell Res. 163 (2), 539-548 (1986)
PUBMED 3007184
REFERENCE 8 (residues 1 to 372)
AUTHORS Lee,M.G., Lewis,S.A., Wilde,C.D. and Cowan,N.J.
TITLE Evolutionary history of a multigene family: an expressed human
beta-tubulin gene and three processed pseudogenes
JOURNAL Cell 33 (2), 477-487 (1983)
PUBMED 6688039
REFERENCE 9 (residues 1 to 372)
AUTHORS Hall,J.L., Dudley,L., Dobner,P.R., Lewis,S.A. and Cowan,N.J.
TITLE Identification of two human beta-tubulin isotypes
JOURNAL Mol. Cell. Biol. 3 (5), 854-862 (1983)
PUBMED 6865944
REFERENCE 10 (residues 1 to 372)
AUTHORS Cowan,N.J., Wilde,C.D., Chow,L.T. and Wefald,F.C.
TITLE Structural variation among human beta-tubulin genes
JOURNAL Proc. Natl. Acad. Sci. U.S.A. 78 (8), 4877-4881 (1981)
PUBMED 6946435
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from DC353572.1, DC405540.1,
AL662797.7, BC013374.2 and BQ019614.1.

Summary: This gene encodes a beta tubulin protein. This protein


forms a dimer with alpha tubulin and acts as a structural
component
of microtubules. Mutations in this gene cause cortical dysplasia,
complex, with other brain malformations 6. Alternative splicing
results in multiple splice variants. There are multiple
pseudogenes
for this gene on chromosomes 1, 6, 7, 8, 9, and 13. [provided by
RefSeq, Jun 2014].

Transcript Variant: This variant (6) lacks a portion of the 5'


coding region and initiates translation at a downstream in-frame
start codon, compared to variant 1. The encoded isoform (e) has a
shorter N-terminus than isoform a. Variants 5 and 6 encode the
same
isoform (e).

Publication Note: This RefSeq record includes a subset of the


publications that are available for this gene. Please see the
Gene
record to access additional publications.
##Evidence-Data-START##
RNAseq introns :: single sample supports all introns
SAMEA2161674,
SAMEA962343 [ECO:0000348]
##Evidence-Data-END##
FEATURES Location/Qualifiers
source 1..372
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="6"
/map="6p21.33"
Protein 1..372
/product="tubulin beta chain isoform e"
/note="beta Ib tubulin; tubulin, beta polypeptide;
tubulin
beta-1 chain; tubulin beta-5 chain; tubulin, beta class
I"
/calculated_mol_wt=41611
Region 1..357
/region_name="PLN00220"
/note="tubulin beta chain; Provisional"
/db_xref="CDD:215107"
Region 1..354
/region_name="beta_tubulin"
/note="The beta-tubulin family; cd02187"
/db_xref="CDD:276956"
Site
order(59,173..175,179,184,186..188,250..252,255,275..279)
/site_type="other"
/note="beta/alpha domain interface [polypeptide
binding]"
/db_xref="CDD:276956"
CDS 1..372
/gene="TUBB"
/gene_synonym="CDCBM6; CSCSC1; M40; OK/SW-cl.56; TUBB1;
TUBB5"
/coded_by="NM_001293216.1:409..1527"
/note="isoform e is encoded by transcript variant 6"
/db_xref="CCDS:CCDS78124.1"
/db_xref="GeneID:203068"
/db_xref="HGNC:HGNC:20778"
/db_xref="MIM:191130"
ORIGIN
1 mdsvrsgpfg qifrpdnfvf gqsgagnnwa kghytegael vdsvldvvrk eaescdclqg
61 fqlthslggg tgsgmgtlli skireeypdr imntfsvvps pkvsdtvvep ynatlsvhql
121 ventdetyci dnealydicf rtlklttpty gdlnhlvsat msgvttclrf pgqlnadlrk
181 lavnmvpfpr lhffmpgfap ltsrgsqqyr altvpeltqq vfdaknmmaa cdprhgrylt
241 vaavfrgrms mkevdeqmln vqnknssyfv ewipnnvkta vcdipprglk mavtfignst
301 aiqelfkris eqftamfrrk aflhwytgeg mdemefteae snmndlvsey qqyqdataee
361 eedfgeeaee ea
//

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