Proteopedia - User contributions [en]

Sandbox my first page 001

2025-11-30T17:07:49Z

Jhanvi Kath: Created full sandbox page for 8VAC: added structure overview, functional analysis, ligand-binding highlights, reference citation, image gallery, and uploaded figure.

= Cryo-EM Structure of Human Serum Albumin (2024) =
''By JHANVI KATH BI3323-Aug 2025''

== Reference Study ==
Catalano C., Lucier K. W., To D., Senko S., Tran N. L., Farwell A. C., Silva S. M., Dip P. V., Poweleit N., Scapin G. (2024).
''The CryoEM structure of human serum albumin in complex with ligands.''
Journal of Structural Biology, 216(3):108105.
DOI: 10.1016/j.jsb.2024.108105

PDB ID: 8VAC

== Structure ==
<StructureSection load='8VAC' size='340' side='right' caption='Cryo-EM structure of human serum albumin bound to ligands (8VAC, 2024)' scene=''>
Human Serum Albumin (HSA) is the dominant plasma protein responsible for transport, buffering, and molecular trafficking.
The 2024 cryo-EM map (8VAC) captures HSA in complex with multiple ligands under near-physiological biochemical conditions, revealing:

* Three-domain organization (I, II, III), each with A/B subdomains.
* A flexible, heart-shaped tertiary fold.
* Multiple hydrophobic binding pockets for drugs, fatty acids, and endogenous molecules.
* Conformational adjustments in Sudlow sites I and II upon ligand engagement.
* Domain movements consistent with adaptive ligand accommodation.

The loaded 8VAC structure provides a solution-like, high-fidelity representation of the molecule.
</StructureSection>

== Function ==
HSA acts as a systemic transport hub in the bloodstream.
Major physiological roles include:

* Binding and transport of fatty acids, bilirubin, hormones, and xenobiotics.
* Strong influence on pharmacokinetics for albumin-bound drugs.
* Maintenance of colloid osmotic pressure.
* Participation in pH buffering and redox balance.

The 8VAC cryo-EM structure highlights how the protein repositions domains to optimize ligand engagement.

== Disease ==
Structural or concentration changes in HSA correlate with many pathologies:

* Hypoalbuminemia in liver disease, sepsis, nephrotic syndrome.
* Glycation and oxidation in diabetes or chronic kidney disease, altering ligand affinity.
* Hereditary albumin variants, impacting stability and drug-binding profiles.
* Altered levels in inflammation, cancer, and severe infection influence drug dosing outcomes.

Structural mapping enables correlation of clinical conditions with ligand-pocket geometry.

== Relevance ==
The 8VAC structure is directly applicable to:

* Drug design – understanding pocket architecture assists affinity and specificity tuning.
* PK/PD modeling – high-affinity albumin binders require dosage fine-tuning.
* Albumin-based drug delivery systems – nanoparticles and small molecules utilize albumin’s long circulation time.
* Biomarker interpretation – albumin concentration is essential in diagnoses and scoring systems.

This structure bridges clinical context and molecular understanding in a single cryo-EM model.

== Structural Highlights ==
Below are placeholder SAT scenes that you can replace with your own:

* Overall 3-domain organization:
<scene name="/sandbox/jhanvi/HSA_8VAC/overall/1">Domain overview</scene>

* Sudlow Site I (Domain IIA):
<scene name="/sandbox/jhanvi/HSA_8VAC/siteI/1">Primary drug-binding pocket</scene>

* Sudlow Site II (Domain IIIA):
<scene name="/sandbox/jhanvi/HSA_8VAC/siteII/1">Secondary drug-binding pocket</scene>

* Flexibility + domain movements:
<scene name="/sandbox/jhanvi/HSA_8VAC/flexibility/1">Hinge flexibility</scene>

== Uploaded Figures ==
Insert your PNGs here after uploading (instructions below):

<gallery>
File:HSA_Overall_Structure.png|Overall Cryo-EM structure of Human Serum Albumin (8VAC)
File:HSA_Salicylic.png|HSA with salicylic ligand bound
</gallery>

== References ==
<references/>

Sandbox:Jhanvi Kath

2025-11-30T17:04:39Z

Jhanvi Kath:

Sandbox:Jhanvi Kath

2025-11-30T17:04:11Z

Jhanvi Kath:

= Cryo-EM Structure of Human Serum Albumin (2024) =
''By JHANVI KATH BI3323-Aug 2025''

== Reference Study ==
Catalano C., Lucier K. W., To D., Senko S., Tran N. L., Farwell A. C., Silva S. M., Dip P. V., Poweleit N., Scapin G. (2024).
''The CryoEM structure of human serum albumin in complex with ligands.''
Journal of Structural Biology, 216(3):108105.
DOI: 10.1016/j.jsb.2024.108105

PDB ID: 8VAC

== Structure ==
<StructureSection load='8VAC' size='340' side='right' caption='Cryo-EM structure of human serum albumin bound to ligands (8VAC, 2024)' scene=''>
Human Serum Albumin (HSA) is the dominant plasma protein responsible for transport, buffering, and molecular trafficking.
The 2024 cryo-EM map (8VAC) captures HSA in complex with multiple ligands under near-physiological biochemical conditions, revealing:

* Three-domain organization (I, II, III), each with A/B subdomains.
* A flexible, heart-shaped tertiary fold.
* Multiple hydrophobic binding pockets for drugs, fatty acids, and endogenous molecules.
* Conformational adjustments in Sudlow sites I and II upon ligand engagement.
* Domain movements consistent with adaptive ligand accommodation.

The loaded 8VAC structure provides a solution-like, high-fidelity representation of the molecule.
</StructureSection>

== Function ==
HSA acts as a systemic transport hub in the bloodstream.
Major physiological roles include:

* Binding and transport of fatty acids, bilirubin, hormones, and xenobiotics.
* Strong influence on pharmacokinetics for albumin-bound drugs.
* Maintenance of colloid osmotic pressure.
* Participation in **pH buffering** and redox balance.

The 8VAC cryo-EM structure highlights how the protein repositions domains to optimize ligand engagement.

== Disease ==
Structural or concentration changes in HSA correlate with many pathologies:

* Hypoalbuminemia in liver disease, sepsis, nephrotic syndrome.
* Glycation and oxidation in diabetes or chronic kidney disease, altering ligand affinity.
* Hereditary albumin variants, impacting stability and drug-binding profiles.
* Altered levels in inflammation, cancer, and severe infection influence drug dosing outcomes.

Structural mapping enables correlation of clinical conditions with ligand-pocket geometry.

== Relevance ==
The 8VAC structure is directly applicable to:

* Drug design – understanding pocket architecture assists affinity and specificity tuning.
* PK/PD modeling – high-affinity albumin binders require dosage fine-tuning.
* Albumin-based drug delivery systems – nanoparticles and small molecules utilize albumin’s long circulation time.
* Biomarker interpretation – albumin concentration is essential in diagnoses and scoring systems.

This structure bridges clinical context and molecular understanding in a single cryo-EM model.

== Structural Highlights ==
Below are placeholder SAT scenes that you can replace with your own:

* Overall 3-domain organization:
<scene name="/sandbox/jhanvi/HSA_8VAC/overall/1">Domain overview</scene>

* Sudlow Site I (Domain IIA):
<scene name="/sandbox/jhanvi/HSA_8VAC/siteI/1">Primary drug-binding pocket</scene>

* Sudlow Site II (Domain IIIA):
<scene name="/sandbox/jhanvi/HSA_8VAC/siteII/1">Secondary drug-binding pocket</scene>

* Flexibility + domain movements:
<scene name="/sandbox/jhanvi/HSA_8VAC/flexibility/1">Hinge flexibility</scene>

== Uploaded Figures ==
Insert your PNGs here after uploading (instructions below):

<gallery>
File:HSA_Overall_Structure.png|Overall Cryo-EM structure of Human Serum Albumin (8VAC)
File:HSA_Salicylic.png|HSA with salicylic ligand bound
</gallery>

== References ==
<references/>

Sandbox:Jhanvi Kath

2025-11-30T14:22:11Z

Jhanvi Kath:

= Cryo-EM Structure of Human Serum Albumin (2024) =
''By JHANVI KATH BI3323-Aug 2025''

== Reference Study ==
Catalano C., Lucier K. W., To D., Senko S., Tran N. L., Farwell A. C., Silva S. M., Dip P. V., Poweleit N., Scapin G. (2024).
''The CryoEM structure of human serum albumin in complex with ligands.''
Journal of Structural Biology, 216(3):108105.
DOI: 10.1016/j.jsb.2024.108105

PDB ID: **8VAC**

== Structure ==
<StructureSection load='8VAC' size='340' side='right' caption='Cryo-EM structure of human serum albumin bound to ligands (8VAC, 2024)' scene=''>
Human Serum Albumin (HSA) is the dominant plasma protein responsible for transport, buffering, and molecular trafficking.
The 2024 cryo-EM map (8VAC) captures HSA in complex with multiple ligands under near-physiological biochemical conditions, revealing:

* Three-domain organization (I, II, III), each with A/B subdomains.
* A flexible, heart-shaped tertiary fold.
* Multiple hydrophobic binding pockets for drugs, fatty acids, and endogenous molecules.
* Conformational adjustments in Sudlow sites I and II upon ligand engagement.
* Domain movements consistent with adaptive ligand accommodation.

The loaded 8VAC structure provides a solution-like, high-fidelity representation of the molecule.
</StructureSection>

== Function ==
HSA acts as a systemic transport hub in the bloodstream.
Major physiological roles include:

* Binding and transport of **fatty acids**, **bilirubin**, hormones, and xenobiotics.
* Strong influence on **pharmacokinetics** for albumin-bound drugs.
* Maintenance of **colloid osmotic pressure**.
* Participation in **pH buffering** and redox balance.

The 8VAC cryo-EM structure highlights how the protein repositions domains to optimize ligand engagement.

== Disease ==
Structural or concentration changes in HSA correlate with many pathologies:

* **Hypoalbuminemia** in liver disease, sepsis, nephrotic syndrome.
* **Glycation and oxidation** in diabetes or chronic kidney disease, altering ligand affinity.
* **Hereditary albumin variants**, impacting stability and drug-binding profiles.
* Altered levels in **inflammation**, **cancer**, and severe infection influence drug dosing outcomes.

Structural mapping enables correlation of clinical conditions with ligand-pocket geometry.

== Relevance ==
The 8VAC structure is directly applicable to:

* **Drug design** – understanding pocket architecture assists affinity and specificity tuning.
* **PK/PD modeling** – high-affinity albumin binders require dosage fine-tuning.
* **Albumin-based drug delivery systems** – nanoparticles and small molecules utilize albumin’s long circulation time.
* **Biomarker interpretation** – albumin concentration is essential in diagnoses and scoring systems.

This structure bridges clinical context and molecular understanding in a single cryo-EM model.

== Structural Highlights ==
Below are placeholder SAT scenes that you can replace with your own:

* Overall 3-domain organization:
<scene name="/sandbox/jhanvi/HSA_8VAC/overall/1">Domain overview</scene>

* Sudlow Site I (Domain IIA):
<scene name="/sandbox/jhanvi/HSA_8VAC/siteI/1">Primary drug-binding pocket</scene>

* Sudlow Site II (Domain IIIA):
<scene name="/sandbox/jhanvi/HSA_8VAC/siteII/1">Secondary drug-binding pocket</scene>

* Flexibility + domain movements:
<scene name="/sandbox/jhanvi/HSA_8VAC/flexibility/1">Hinge flexibility</scene>

== Uploaded Figures ==
Insert your PNGs here after uploading (instructions below):

<gallery>
File:HSA_Overall_Structure.png|Overall Cryo-EM structure of Human Serum Albumin (8VAC)
File:HSA_Salicylic.png|HSA with salicylic ligand bound
</gallery>

== References ==
<references/>

Sandbox:Jhanvi Kath

2025-11-30T14:20:28Z

Jhanvi Kath:

= Cryo-EM Structure of Human Serum Albumin (2024) =
''By JHANVI''

== Reference Study ==
Catalano C., Lucier K. W., To D., Senko S., Tran N. L., Farwell A. C., Silva S. M., Dip P. V., Poweleit N., Scapin G. (2024).
''The CryoEM structure of human serum albumin in complex with ligands.''
Journal of Structural Biology, 216(3):108105.
DOI: 10.1016/j.jsb.2024.108105

PDB ID: **8VAC**

== Structure ==
<StructureSection load='8VAC' size='340' side='right' caption='Cryo-EM structure of human serum albumin bound to ligands (8VAC, 2024)' scene=''>
Human Serum Albumin (HSA) is the dominant plasma protein responsible for transport, buffering, and molecular trafficking.
The 2024 cryo-EM map (8VAC) captures HSA in complex with multiple ligands under near-physiological biochemical conditions, revealing:

* Three-domain organization (I, II, III), each with A/B subdomains.
* A flexible, heart-shaped tertiary fold.
* Multiple hydrophobic binding pockets for drugs, fatty acids, and endogenous molecules.
* Conformational adjustments in Sudlow sites I and II upon ligand engagement.
* Domain movements consistent with adaptive ligand accommodation.

The loaded 8VAC structure provides a solution-like, high-fidelity representation of the molecule.
</StructureSection>

== Function ==
HSA acts as a systemic transport hub in the bloodstream.
Major physiological roles include:

* Binding and transport of **fatty acids**, **bilirubin**, hormones, and xenobiotics.
* Strong influence on **pharmacokinetics** for albumin-bound drugs.
* Maintenance of **colloid osmotic pressure**.
* Participation in **pH buffering** and redox balance.

The 8VAC cryo-EM structure highlights how the protein repositions domains to optimize ligand engagement.

== Disease ==
Structural or concentration changes in HSA correlate with many pathologies:

* **Hypoalbuminemia** in liver disease, sepsis, nephrotic syndrome.
* **Glycation and oxidation** in diabetes or chronic kidney disease, altering ligand affinity.
* **Hereditary albumin variants**, impacting stability and drug-binding profiles.
* Altered levels in **inflammation**, **cancer**, and severe infection influence drug dosing outcomes.

Structural mapping enables correlation of clinical conditions with ligand-pocket geometry.

== Relevance ==
The 8VAC structure is directly applicable to:

* **Drug design** – understanding pocket architecture assists affinity and specificity tuning.
* **PK/PD modeling** – high-affinity albumin binders require dosage fine-tuning.
* **Albumin-based drug delivery systems** – nanoparticles and small molecules utilize albumin’s long circulation time.
* **Biomarker interpretation** – albumin concentration is essential in diagnoses and scoring systems.

This structure bridges clinical context and molecular understanding in a single cryo-EM model.

== Structural Highlights ==
Below are placeholder SAT scenes that you can replace with your own:

* Overall 3-domain organization:
<scene name="/sandbox/jhanvi/HSA_8VAC/overall/1">Domain overview</scene>

* Sudlow Site I (Domain IIA):
<scene name="/sandbox/jhanvi/HSA_8VAC/siteI/1">Primary drug-binding pocket</scene>

* Sudlow Site II (Domain IIIA):
<scene name="/sandbox/jhanvi/HSA_8VAC/siteII/1">Secondary drug-binding pocket</scene>

* Flexibility + domain movements:
<scene name="/sandbox/jhanvi/HSA_8VAC/flexibility/1">Hinge flexibility</scene>

== Uploaded Figures ==
Insert your PNGs here after uploading (instructions below):

<gallery>
File:HSA_Overall_Structure.png|Overall Cryo-EM structure of Human Serum Albumin (8VAC)
File:HSA_Salicylic.png|HSA with salicylic ligand bound
</gallery>

== References ==
<references/>

File:HSA Overall Structure.png

2025-11-30T14:19:27Z

Jhanvi Kath: uploaded a new version of "Image:HSA Overall Structure.png"

Sandbox:Jhanvi Kath

2025-11-30T14:19:03Z

Jhanvi Kath: New page: ==Your Heading Here (maybe something like 'Structure')== <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> This is a default text for you...

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox:Jhanvi Kath'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

CreateSandbox

2025-11-30T14:14:28Z

Jhanvi Kath:

= Cryo-EM Structure of Human Serum Albumin (2024) =
''By JHANVI''

== Reference Study ==
Catalano C., Lucier K. W., To D., Senko S., Tran N. L., Farwell A. C., Silva S. M., Dip P. V., Poweleit N., Scapin G. (2024).
''The CryoEM structure of human serum albumin in complex with ligands.''
Journal of Structural Biology, 216(3):108105.
DOI: 10.1016/j.jsb.2024.108105

PDB ID: **8VAC**

== Structure ==
<StructureSection load='8VAC' size='340' side='right' caption='Cryo-EM structure of human serum albumin bound to ligands (8VAC, 2024)' scene=''>
Human Serum Albumin (HSA) is the dominant plasma protein responsible for transport, buffering, and molecular trafficking.
The 2024 cryo-EM map (8VAC) captures HSA in complex with multiple ligands under near-physiological biochemical conditions, revealing:

* Three-domain organization (I, II, III), each with A/B subdomains.
* A flexible, heart-shaped tertiary fold.
* Multiple hydrophobic binding pockets for drugs, fatty acids, and endogenous molecules.
* Conformational adjustments in Sudlow sites I and II upon ligand engagement.
* Domain movements consistent with adaptive ligand accommodation.

The loaded 8VAC structure provides a solution-like, high-fidelity representation of the molecule.
</StructureSection>

== Function ==
HSA acts as a systemic transport hub in the bloodstream.
Major physiological roles include:

* Binding and transport of **fatty acids**, **bilirubin**, hormones, and xenobiotics.
* Strong influence on **pharmacokinetics** for albumin-bound drugs.
* Maintenance of **colloid osmotic pressure**.
* Participation in **pH buffering** and redox balance.

The 8VAC cryo-EM structure highlights how the protein repositions domains to optimize ligand engagement.

== Disease ==
Structural or concentration changes in HSA correlate with many pathologies:

* **Hypoalbuminemia** in liver disease, sepsis, nephrotic syndrome.
* **Glycation and oxidation** in diabetes or chronic kidney disease, altering ligand affinity.
* **Hereditary albumin variants**, impacting stability and drug-binding profiles.
* Altered levels in **inflammation**, **cancer**, and severe infection influence drug dosing outcomes.

Structural mapping enables correlation of clinical conditions with ligand-pocket geometry.

== Relevance ==
The 8VAC structure is directly applicable to:

* **Drug design** – understanding pocket architecture assists affinity and specificity tuning.
* **PK/PD modeling** – high-affinity albumin binders require dosage fine-tuning.
* **Albumin-based drug delivery systems** – nanoparticles and small molecules utilize albumin’s long circulation time.
* **Biomarker interpretation** – albumin concentration is essential in diagnoses and scoring systems.

This structure bridges clinical context and molecular understanding in a single cryo-EM model.

== Structural Highlights ==
Below are placeholder SAT scenes that you can replace with your own:

* Overall 3-domain organization:
<scene name="/sandbox/jhanvi/HSA_8VAC/overall/1">Domain overview</scene>

* Sudlow Site I (Domain IIA):
<scene name="/sandbox/jhanvi/HSA_8VAC/siteI/1">Primary drug-binding pocket</scene>

* Sudlow Site II (Domain IIIA):
<scene name="/sandbox/jhanvi/HSA_8VAC/siteII/1">Secondary drug-binding pocket</scene>

* Flexibility + domain movements:
<scene name="/sandbox/jhanvi/HSA_8VAC/flexibility/1">Hinge flexibility</scene>

== Uploaded Figures ==

<gallery>
File: HSA_Overall_Structure.png|Overall Cryo-EM structure of HSA (8VAC)
File: HSA+Salicylic.png|HSA with salicylic ligand bound
</gallery>

== References ==
<references/>

File:HSA + Salicyclic.png

2025-11-30T14:12:57Z

Jhanvi Kath:

CreateSandbox

2025-11-30T14:12:30Z

Jhanvi Kath:

= Cryo-EM Structure of Human Serum Albumin (2024) =
''By JHANVI''

== Reference Study ==
Catalano C., Lucier K. W., To D., Senko S., Tran N. L., Farwell A. C., Silva S. M., Dip P. V., Poweleit N., Scapin G. (2024).
''The CryoEM structure of human serum albumin in complex with ligands.''
Journal of Structural Biology, 216(3):108105.
DOI: 10.1016/j.jsb.2024.108105

PDB ID: **8VAC**

== Structure ==
<StructureSection load='8VAC' size='340' side='right' caption='Cryo-EM structure of human serum albumin bound to ligands (8VAC, 2024)' scene=''>
Human Serum Albumin (HSA) is the dominant plasma protein responsible for transport, buffering, and molecular trafficking.
The 2024 cryo-EM map (8VAC) captures HSA in complex with multiple ligands under near-physiological biochemical conditions, revealing:

* Three-domain organization (I, II, III), each with A/B subdomains.
* A flexible, heart-shaped tertiary fold.
* Multiple hydrophobic binding pockets for drugs, fatty acids, and endogenous molecules.
* Conformational adjustments in Sudlow sites I and II upon ligand engagement.
* Domain movements consistent with adaptive ligand accommodation.

The loaded 8VAC structure provides a solution-like, high-fidelity representation of the molecule.
</StructureSection>

== Function ==
HSA acts as a systemic transport hub in the bloodstream.
Major physiological roles include:

* Binding and transport of **fatty acids**, **bilirubin**, hormones, and xenobiotics.
* Strong influence on **pharmacokinetics** for albumin-bound drugs.
* Maintenance of **colloid osmotic pressure**.
* Participation in **pH buffering** and redox balance.

The 8VAC cryo-EM structure highlights how the protein repositions domains to optimize ligand engagement.

== Disease ==
Structural or concentration changes in HSA correlate with many pathologies:

* **Hypoalbuminemia** in liver disease, sepsis, nephrotic syndrome.
* **Glycation and oxidation** in diabetes or chronic kidney disease, altering ligand affinity.
* **Hereditary albumin variants**, impacting stability and drug-binding profiles.
* Altered levels in **inflammation**, **cancer**, and severe infection influence drug dosing outcomes.

Structural mapping enables correlation of clinical conditions with ligand-pocket geometry.

== Relevance ==
The 8VAC structure is directly applicable to:

* **Drug design** – understanding pocket architecture assists affinity and specificity tuning.
* **PK/PD modeling** – high-affinity albumin binders require dosage fine-tuning.
* **Albumin-based drug delivery systems** – nanoparticles and small molecules utilize albumin’s long circulation time.
* **Biomarker interpretation** – albumin concentration is essential in diagnoses and scoring systems.

This structure bridges clinical context and molecular understanding in a single cryo-EM model.

== Structural Highlights ==
Below are placeholder SAT scenes that you can replace with your own:

* Overall 3-domain organization:
<scene name="/sandbox/jhanvi/HSA_8VAC/overall/1">Domain overview</scene>

* Sudlow Site I (Domain IIA):
<scene name="/sandbox/jhanvi/HSA_8VAC/siteI/1">Primary drug-binding pocket</scene>

* Sudlow Site II (Domain IIIA):
<scene name="/sandbox/jhanvi/HSA_8VAC/siteII/1">Secondary drug-binding pocket</scene>

* Flexibility + domain movements:
<scene name="/sandbox/jhanvi/HSA_8VAC/flexibility/1">Hinge flexibility</scene>

== Uploaded Figures ==

<gallery>
File: HSA_Overall_Structure.png|Overall Cryo-EM structure of HSA (8VAC)
</gallery>

== References ==
<references/>

File:HSA Overall Structure.png

2025-11-30T14:06:11Z

Jhanvi Kath:

CreateSandbox

2025-11-30T14:05:16Z

Jhanvi Kath: New page: = Cryo-EM Structure of Human Serum Albumin (2024) = ''By JHANVI'' == Reference Study == Catalano C., Lucier K. W., To D., Senko S., Tran N. L., Farwell A. C., Silva S. M., Dip P. V., Powe...

= Cryo-EM Structure of Human Serum Albumin (2024) =
''By JHANVI''

== Reference Study ==
Catalano C., Lucier K. W., To D., Senko S., Tran N. L., Farwell A. C., Silva S. M., Dip P. V., Poweleit N., Scapin G. (2024).
''The CryoEM structure of human serum albumin in complex with ligands.''
Journal of Structural Biology, 216(3):108105.
DOI: 10.1016/j.jsb.2024.108105

PDB ID: **8VAC**

== Structure ==
<StructureSection load='8VAC' size='340' side='right' caption='Cryo-EM structure of human serum albumin bound to ligands (8VAC, 2024)' scene=''>
Human Serum Albumin (HSA) is the dominant plasma protein responsible for transport, buffering, and molecular trafficking.
The 2024 cryo-EM map (8VAC) captures HSA in complex with multiple ligands under near-physiological biochemical conditions, revealing:

* Three-domain organization (I, II, III), each with A/B subdomains.
* A flexible, heart-shaped tertiary fold.
* Multiple hydrophobic binding pockets for drugs, fatty acids, and endogenous molecules.
* Conformational adjustments in Sudlow sites I and II upon ligand engagement.
* Domain movements consistent with adaptive ligand accommodation.

The loaded 8VAC structure provides a solution-like, high-fidelity representation of the molecule.
</StructureSection>

== Function ==
HSA acts as a systemic transport hub in the bloodstream.
Major physiological roles include:

* Binding and transport of **fatty acids**, **bilirubin**, hormones, and xenobiotics.
* Strong influence on **pharmacokinetics** for albumin-bound drugs.
* Maintenance of **colloid osmotic pressure**.
* Participation in **pH buffering** and redox balance.

The 8VAC cryo-EM structure highlights how the protein repositions domains to optimize ligand engagement.

== Disease ==
Structural or concentration changes in HSA correlate with many pathologies:

* **Hypoalbuminemia** in liver disease, sepsis, nephrotic syndrome.
* **Glycation and oxidation** in diabetes or chronic kidney disease, altering ligand affinity.
* **Hereditary albumin variants**, impacting stability and drug-binding profiles.
* Altered levels in **inflammation**, **cancer**, and severe infection influence drug dosing outcomes.

Structural mapping enables correlation of clinical conditions with ligand-pocket geometry.

== Relevance ==
The 8VAC structure is directly applicable to:

* **Drug design** – understanding pocket architecture assists affinity and specificity tuning.
* **PK/PD modeling** – high-affinity albumin binders require dosage fine-tuning.
* **Albumin-based drug delivery systems** – nanoparticles and small molecules utilize albumin’s long circulation time.
* **Biomarker interpretation** – albumin concentration is essential in diagnoses and scoring systems.

This structure bridges clinical context and molecular understanding in a single cryo-EM model.

== Structural Highlights ==
Below are placeholder SAT scenes that you can replace with your own:

* Overall 3-domain organization:
<scene name="/sandbox/jhanvi/HSA_8VAC/overall/1">Domain overview</scene>

* Sudlow Site I (Domain IIA):
<scene name="/sandbox/jhanvi/HSA_8VAC/siteI/1">Primary drug-binding pocket</scene>

* Sudlow Site II (Domain IIIA):
<scene name="/sandbox/jhanvi/HSA_8VAC/siteII/1">Secondary drug-binding pocket</scene>

* Flexibility + domain movements:
<scene name="/sandbox/jhanvi/HSA_8VAC/flexibility/1">Hinge flexibility</scene>

== Uploaded Figures ==
Insert your PNGs here after uploading (instructions below):

<gallery>
File:YourImage1.png|Cryo-EM map overview
File:YourImage2.png|Ligand-binding pockets highlighted
</gallery>

== References ==
<references/>

Sandbox my-first page 001

2025-11-30T12:58:05Z

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox my-first page 001'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>