1rjb: Difference between revisions

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[[Image:1rjb.gif|left|200px]]<br />

[[Image:1rjb.gif|left|200px]]<br /><applet load="1rjb" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1rjb" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1rjb, resolution 2.10Å" />

'''Crystal Structure of FLT3'''<br />

==Overview==

FLT3 is a type III receptor tyrosine kinase that is thought to play a key, role in hematopoiesis. Certain classes of FLT3 mutations cause, constitutively activated forms of the receptor that are found in, significant numbers of patients with acute myelogenous leukemia (AML). The, mutations occur either in the activation loop, for example, as point, mutations of Asp835 or as internal tandem duplication (ITD) sequences in, the juxtamembrane (JM) domain. To further understand the nature of FLT3, autoinhibition and regulation, we have determined the crystal structure of, the autoinhibited form of FLT3. This structure shows the autoinhibitory, conformation of a complete JM domain in this class of receptor tyrosine, kinases. The detailed inhibitory mechanism of the JM domain is revealed, which is likely utilized by other members of type III receptor tyrosine, kinases.

FLT3 is a type III receptor tyrosine kinase that is thought to play a key role in hematopoiesis. Certain classes of FLT3 mutations cause constitutively activated forms of the receptor that are found in significant numbers of patients with acute myelogenous leukemia (AML). The mutations occur either in the activation loop, for example, as point mutations of Asp835 or as internal tandem duplication (ITD) sequences in the juxtamembrane (JM) domain. To further understand the nature of FLT3 autoinhibition and regulation, we have determined the crystal structure of the autoinhibited form of FLT3. This structure shows the autoinhibitory conformation of a complete JM domain in this class of receptor tyrosine kinases. The detailed inhibitory mechanism of the JM domain is revealed, which is likely utilized by other members of type III receptor tyrosine kinases.

==Disease==

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==About this Structure==

1RJB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1RJB OCA].

1RJB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RJB OCA].

==Reference==

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[[Category: structure]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 19~~:04:28 ~~2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:51:28 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1rjb.gif|left|200px]]<br />
+[[Image:1rjb.gif|left|200px]]<br /><applet load="1rjb" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1rjb" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1rjb, resolution 2.10&Aring;" />
 '''Crystal Structure of FLT3'''<br />
 ==Overview==
-FLT3 is a type III receptor tyrosine kinase that is thought to play a key, role in hematopoiesis. Certain classes of FLT3 mutations cause, constitutively activated forms of the receptor that are found in, significant numbers of patients with acute myelogenous leukemia (AML). The, mutations occur either in the activation loop, for example, as point, mutations of Asp835 or as internal tandem duplication (ITD) sequences in, the juxtamembrane (JM) domain. To further understand the nature of FLT3, autoinhibition and regulation, we have determined the crystal structure of, the autoinhibited form of FLT3. This structure shows the autoinhibitory, conformation of a complete JM domain in this class of receptor tyrosine, kinases. The detailed inhibitory mechanism of the JM domain is revealed, which is likely utilized by other members of type III receptor tyrosine, kinases.
+FLT3 is a type III receptor tyrosine kinase that is thought to play a key role in hematopoiesis. Certain classes of FLT3 mutations cause constitutively activated forms of the receptor that are found in significant numbers of patients with acute myelogenous leukemia (AML). The mutations occur either in the activation loop, for example, as point mutations of Asp835 or as internal tandem duplication (ITD) sequences in the juxtamembrane (JM) domain. To further understand the nature of FLT3 autoinhibition and regulation, we have determined the crystal structure of the autoinhibited form of FLT3. This structure shows the autoinhibitory conformation of a complete JM domain in this class of receptor tyrosine kinases. The detailed inhibitory mechanism of the JM domain is revealed, which is likely utilized by other members of type III receptor tyrosine kinases.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-RJB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RJB OCA].
+RJB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RJB OCA].
 ==Reference==
@@ Line 31: / Line 30: @@
 [[Category: structure]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:04:28 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:51:28 2008''