Target Name: DEFA5
NCBI ID: G1670
Review Report on DEFA5 Target / Biomarker Content of Review Report on DEFA5 Target / Biomarker
DEFA5
Other Name(s): defensin, alpha 5, preproprotein | defensin, alpha 5, Paneth cell-specific | DEF5 | HD5(56-94) | HD-5 | HD5(63-94) | HD5(56-94) | Defensin, alpha 5 | DEF5_HUMAN | defensin alpha 5 | Defensin alpha 5 | HD5(23-94) | HD5(29-94) | HD5(20-94) | Defensin-5 | Defensin 5 | HD5(29-94) | HD5(23-94) | HD5(63-94) | defensin-5 | HD5(20-94)

DEFA5: A Potential Drug Target and Biomarker

DEFA5 is a protein that is expressed in various tissues of the body, including the brain, heart, and kidneys. Its full name is doublecortin-like peptide 5, and it is characterized by its unique structure, which consists of two distinct domains: a N-terminal domain and a C-terminal domain. The N-terminal domain contains a highly conserved helical region that is known for its ability to interact with various signaling molecules, while the C-terminal domain contains a highly conserved alkaline site that is involved in the regulation of ion channels.

Recent studies have identified DEFA5 as a potential drug target and biomarker. Its unique structure and the involvement of its C-terminal domain in the regulation of ion channels make it an attractive target for small molecules. Additionally, its expression in various tissues make it a potential biomarker for a variety of diseases.

The Structure of DEFA5

The DEFA5 protein has a molecular weight of approximately 43 kDa and a pre-folded structure of approximately 180 amino acids. The protein is composed of two distinct domains: the N-terminal domain and the C-terminal domain.

The N-terminal domain is a highly conserved region that is known for its ability to interact with various signaling molecules, including casein kinase (Ca2+) and neurotransmitters. The N-terminal domain consists of a single helical region that is approximately 12 amino acids in length. This region is characterized by a variety of conserved motifs, including a nucleotide-binding oligomerization domain (NBO), a putative nucleotide-binding oligomerization domain (NBO), and a zinc finger domain (ZFD).

The C-terminal domain is also a highly conserved region that is involved in the regulation of ion channels. The C-terminal domain consists of a single alpha-helic acid that is approximately 60 amino acids in length. This region is characterized by a variety of conserved motifs, including a nucleotide-binding oligomerization domain (NBO), a putative nucleotide-binding oligomerization domain (NBO), and a zinc finger domain (ZFD).

The Expression of DEFA5

DEFA5 is expressed in a variety of tissues and organs, including the brain, heart, and kidneys. Its expression is highly dependent on the tissue type and is regulated by various factors, including cytokines and signaling molecules.

In the brain, DEFA5 is expressed in the frontal cortex, basal ganglia, and cerebellum. It is also expressed in the heart and kidneys, and its expression is regulated by factors such as neurotransmitters, casein kinase, and calcitonin.

The Potential Role of DEFA5 as a Drug Target

The unique structure of DEFA5 and its expression in various tissues make it an attractive target for small molecules. Its N-terminal domain is known for its ability to interact with various signaling molecules, and its C-terminal domain is involved in the regulation of ion channels. These properties make it an attractive target for small molecules that can modulate its activity.

One potential approach to targeting DEFA5 is to use small molecules that can modulate its activity in a specific manner. For example, one approach could be to use small molecules that interact with the N-terminal domain to modulate its activity, while another approach could be to use small molecules that interact with the C-terminal domain to modulate its activity.

The Potential Role of DEFA5 as a Biomarker

The expression of DEFA5 in various tissues makes it a potential biomarker for a variety of diseases. Its expression is regulated by various factors, including neurotransmitters and signaling molecules, making it an attractive target for biomarkers that can be used to diagnose or

Protein Name: Defensin Alpha 5

Functions: Host-defense peptide that maintains sterility in the urogenital system (PubMed:12021776, PubMed:12660734, PubMed:15616305, PubMed:22359618, PubMed:25354318, PubMed:30808760, PubMed:19589339, PubMed:22573326, PubMed:25782105). Has antimicrobial activity against a wide range of bacteria, including Gram-negative E.coli, P.aeruginosa and S.typhimurium, and Gram-positive E.aerogenes, S.aureus, B.cereus, E.faecium and L.monocytogenes (PubMed:12021776, PubMed:15616305, PubMed:22359618, PubMed:25354318, PubMed:30808760, PubMed:19589339, PubMed:22573326). Confers resistance to intestinal infection by S.typhimurium (PubMed:12660734). Exhibits antimicrobial activity against enteric commensal bacteria such as B.adolescentis, L.acidophilus, B.breve, L.fermentum, B.longum and S.thermophilus (PubMed:25354318). Binds to bacterial membranes and causes membrane disintegration (PubMed:25782105). Induces the secretion of the chemokine IL-8 by intestinal epithelial cells (PubMed:19589339). Binds to B.antracis lef/lethal factor, a major virulence factor from B.anthracis, and neutralizes its enzymatic activity (PubMed:22573326)

The "DEFA5 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about DEFA5 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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DEFA6 | DEFA7P | DEFA8P | DEFA9P | DEFB1 | DEFB103A | DEFB103B | DEFB104A | DEFB104B | DEFB105A | DEFB105B | DEFB106A | DEFB106B | DEFB107A | DEFB108B | DEFB108F | DEFB109A | DEFB109B | DEFB109C | DEFB110 | DEFB112 | DEFB113 | DEFB114 | DEFB115 | DEFB116 | DEFB118 | DEFB119 | DEFB121 | DEFB122 | DEFB123 | DEFB124 | DEFB125 | DEFB126 | DEFB127 | DEFB128 | DEFB129 | DEFB130A | DEFB131A | DEFB131B | DEFB132 | DEFB133 | DEFB134 | DEFB135 | DEFB136 | DEFB4A | DEFB4B | Defensin | DEFT1P | DEFT1P2 | DEGS1 | DEGS2 | DEK | DELE1 | DELEC1 | DENND10 | DENND10P1 | DENND11 | DENND1A | DENND1B | DENND1C | DENND2A | DENND2B | DENND2C | DENND2D | DENND3 | DENND4A | DENND4B | DENND4C | DENND5A | DENND5B | DENND6A | DENND6B | DENR | DEPDC1 | DEPDC1-AS1 | DEPDC1B | DEPDC4 | DEPDC5 | DEPDC7 | DEPP1 | DEPTOR | DERA | DERL1 | DERL2 | DERL3 | DES | DESI1 | DESI2 | DET1 | DEUP1 | DEXI | DFFA | DFFB | DGAT1 | DGAT2 | DGAT2L6 | DGCR11 | DGCR2 | DGCR5 | DGCR6