Interferon-induced guanylate-binding protein 1 is a
protein that in humans is encoded by the GBP1gene.[3][4] It belongs to the
dynamin superfamily of large
GTPases.[5]
Function
Guanylate binding protein expression is induced by
interferon. Guanylate binding proteins are characterized by their ability to specifically bind guanine nucleotides (GMP, GDP, and GTP) and are distinguished from the GTP-binding proteins by the presence of 2 binding motifs rather than 3.[4]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Strehlow I, Lohmann-Matthes ML, Decker T (Aug 1994). "The interferon-inducible GBP1 gene: structure and mapping to human chromosome 1". Gene. 144 (2): 295–9.
doi:
10.1016/0378-1119(94)90393-X.
PMID7518790.
Nantais DE, Schwemmle M, Stickney JT, et al. (1996). "Prenylation of an interferon-gamma-induced GTP-binding protein: the human guanylate binding protein, huGBP1". J. Leukoc. Biol. 60 (3): 423–31.
doi:
10.1002/jlb.60.3.423.
PMID8830800.
S2CID33727864.
Praefcke GJ, Kloep S, Benscheid U, et al. (2004). "Identification of residues in the human guanylate-binding protein 1 critical for nucleotide binding and cooperative GTP hydrolysis". J. Mol. Biol. 344 (1): 257–69.
doi:
10.1016/j.jmb.2004.09.026.
PMID15504415.
1dg3: STRUCTURE OF HUMAN GUANYLATE BINDING PROTEIN-1 IN NUCLEOTIDE FREE FORM
1f5n: HUMAN GUANYLATE BINDING PROTEIN-1 IN COMPLEX WITH THE GTP ANALOGUE, GMPPNP.
2b8w: Crystal-structure of the N-terminal Large GTPase Domain of human Guanylate Binding protein 1 (hGBP1) in complex with GMP/AlF4
2b92: Crystal-structure of the N-terminal Large GTPase Domain of human Guanylate Binding protein 1 (hGBP1) in complex with GDP/AlF3
2bc9: Crystal-structure of the N-terminal large GTPase Domain of human Guanylate Binding protein 1 (hGBP1) in complex with non-hydrolysable GTP analogue GppNHp
2d4h: Crystal-structure of the N-terminal large GTPase Domain of human Guanylate Binding protein 1 (hGBP1) in complex with GMP
Interferon-induced guanylate-binding protein 1 is a
protein that in humans is encoded by the GBP1gene.[3][4] It belongs to the
dynamin superfamily of large
GTPases.[5]
Function
Guanylate binding protein expression is induced by
interferon. Guanylate binding proteins are characterized by their ability to specifically bind guanine nucleotides (GMP, GDP, and GTP) and are distinguished from the GTP-binding proteins by the presence of 2 binding motifs rather than 3.[4]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Strehlow I, Lohmann-Matthes ML, Decker T (Aug 1994). "The interferon-inducible GBP1 gene: structure and mapping to human chromosome 1". Gene. 144 (2): 295–9.
doi:
10.1016/0378-1119(94)90393-X.
PMID7518790.
Nantais DE, Schwemmle M, Stickney JT, et al. (1996). "Prenylation of an interferon-gamma-induced GTP-binding protein: the human guanylate binding protein, huGBP1". J. Leukoc. Biol. 60 (3): 423–31.
doi:
10.1002/jlb.60.3.423.
PMID8830800.
S2CID33727864.
Praefcke GJ, Kloep S, Benscheid U, et al. (2004). "Identification of residues in the human guanylate-binding protein 1 critical for nucleotide binding and cooperative GTP hydrolysis". J. Mol. Biol. 344 (1): 257–69.
doi:
10.1016/j.jmb.2004.09.026.
PMID15504415.
1dg3: STRUCTURE OF HUMAN GUANYLATE BINDING PROTEIN-1 IN NUCLEOTIDE FREE FORM
1f5n: HUMAN GUANYLATE BINDING PROTEIN-1 IN COMPLEX WITH THE GTP ANALOGUE, GMPPNP.
2b8w: Crystal-structure of the N-terminal Large GTPase Domain of human Guanylate Binding protein 1 (hGBP1) in complex with GMP/AlF4
2b92: Crystal-structure of the N-terminal Large GTPase Domain of human Guanylate Binding protein 1 (hGBP1) in complex with GDP/AlF3
2bc9: Crystal-structure of the N-terminal large GTPase Domain of human Guanylate Binding protein 1 (hGBP1) in complex with non-hydrolysable GTP analogue GppNHp
2d4h: Crystal-structure of the N-terminal large GTPase Domain of human Guanylate Binding protein 1 (hGBP1) in complex with GMP